Journal articles: 'Kinesin superfamily protein'

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Park, Hye-Young, Sang-Jin Kim, Sung-Su Ye, Won-Hee Jang, Sang-Kyeong Lee, Yeong-Hong Park, Yong-Wook Jung, Il-Soo Moon, Moo-Seong Kim, and Dae-Hyun Seog. "Pcp-2 Interacts Directly with Kinesin Superfamily KIF21A Protein." Journal of Life Science 18, no. 8 (August 30, 2008): 1059–65. http://dx.doi.org/10.5352/jls.2008.18.8.1059.

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Jang, Won Hee, and Dae-Hyun Seog. "Kinesin Superfamily-associated Protein 3 (KAP3) Mediates the Interaction between Kinesin-II Motor Subunits and HS-1-associated Protein X-1 (HAX-1) through Direct Binding." Journal of Life Science 23, no. 8 (August 30, 2013): 978–83. http://dx.doi.org/10.5352/jls.2013.23.8.978.

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Wong-Riley, Margaret T. T., and Joseph C. Besharse. "The kinesin superfamily protein KIF17: one protein with many functions." BioMolecular Concepts 3, no. 3 (June 1, 2012): 267–82. http://dx.doi.org/10.1515/bmc-2011-0064.

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AbstractKinesins are ATP-dependent molecular motors that carry cargos along microtubules, generally in an anterograde direction. They are classified into 14 distinct families with varying structural and functional characteristics. KIF17 is a member of the kinesin-2 family that is plus end-directed. It is a homodimer with a pair of head motor domains that bind microtubules, a coiled-coil stalk, and a tail domain that binds cargos. In neurons, KIF17 transports N-methyl-D-aspartate receptor NR2B subunit, kainate receptor GluR5, and potassium Kv4.2 channels from cell bodies exclusively to dendrites. These cargos are necessary for synaptic transmission, learning, memory and other functions. KIF17’s interaction with nuclear RNS export factor 2 (NXF2) enables the transport of mRNA bidirectionally in dendrites. KIF17 or its homolog osmotic avoidance abnormal protein 3 (OSM-3) also mediates intraflagellar transport of cargos to the distal tips of flagella or cilia, thereby aiding in ciliogenesis. In many invertebrate and vertebrate sensory cells, KIF17 delivers cargos that contribute to chemosensory perception and signal transduction. In vertebrate photoreceptors, KIF17 is necessary for outer segment development and disc morphogenesis. In the testis, KIF17 (KIF17b) mediates microtubule-independent delivery of an activator of cAMP-responsive element modulator (ACT) from the nucleus to the cytoplasm and microtubule-dependent transport of Spatial-ε, both are presumably involved in spermatogenesis. KIF17 is also implicated in epithelial polarity and morphogenesis, placental transport and development, and the development of specific brain regions. The transcriptional regulation of Kif17 has recently been found to be mediated by nuclear respiratory factor 1 (NRF-1), which also regulates NR2B as well as energy metabolism in neurons. Dysfunctions of KIF17 are linked to a number of pathologies.

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Hares, K., K. Kemp, C. Rice, E. Gray, N. Scolding, and A. Wilkins. "Reduced axonal motor protein expression in non-lesional grey matter in multiple sclerosis." Multiple Sclerosis Journal 20, no. 7 (October 21, 2013): 812–21. http://dx.doi.org/10.1177/1352458513508836.

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Background: Multiple sclerosis (MS) is a neurological disease characterised by central nervous system inflammation, demyelination, axonal degeneration and neuronal injury. Preventing neuronal and axon damage is of paramount importance in attempts to prevent disease progression. Intact axonal transport mechanisms are crucial to axonal integrity and evidence suggests these mechanisms are disrupted in MS. Anterograde axonal transport is mediated to a large extent through the kinesin superfamily proteins. Recently, certain kinesin superfamily proteins (KIF5A, KIF1B and KIF21B) were implicated in MS pathology. Objectives: To investigate the expression of KIF5A, KIF21B and KIF1B in MS and control post-mortem grey matter. Methods: Using both quantitative real-time polymerase chain reaction (PCR) and Immunodot-blots assays, we analysed the expression of kinesin superfamily proteins in 27 MS cases and 13 control cases not linked to neurological disease. Results: We have shown significant reductions in KIF5A, KIF21B and KIF1B messenger ribonucleic acid (mRNA) expression and also KIF5A protein expression in MS grey matter, as compared to control grey matter. Conclusion: We have shown significant reductions in mRNA and protein levels of axonal motor proteins in the grey matter of MS cases, which may have important implications for the pathogenesis of neuronal/axonal injury in the disease.

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Barrett, Jennifer G., Brendan D. Manning, and Michael Snyder. "The Kar3p Kinesin-related Protein Forms a Novel Heterodimeric Structure with Its Associated Protein Cik1p." Molecular Biology of the Cell 11, no. 7 (July 2000): 2373–85. http://dx.doi.org/10.1091/mbc.11.7.2373.

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Proteins that physically associate with members of the kinesin superfamily are critical for the functional diversity observed for these microtubule motor proteins. However, quaternary structures of complexes between kinesins and kinesin-associated proteins are poorly defined. We have analyzed the nature of the interaction between the Kar3 motor protein, a minus-end–directed kinesin from yeast, and its associated protein Cik1. Extraction experiments demonstrate that Kar3p and Cik1p are tightly associated. Mapping of the interaction domains of the two proteins by two-hybrid analyses indicates that Kar3p and Cik1p associate in a highly specific manner along the lengths of their respective coiled-coil domains. Sucrose gradient velocity centrifugation and gel filtration experiments were used to determine the size of the Kar3-Cik1 complex from both mating pheromone-treated cells and vegetatively growing cells. These experiments predict a size for this complex that is consistent with that of a heterodimer containing one Kar3p subunit and one Cik1p subunit. Finally, immunoprecipitation of epitope-tagged and untagged proteins confirms that only one subunit of Kar3p and Cik1p are present in the Kar3-Cik1 complex. These findings demonstrate that the Kar3-Cik1 complex has a novel heterodimeric structure not observed previously for kinesin complexes.

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Alphey, Luke, Louise Parker, Gillian Hawcroft, Yiquan Guo, Kim Kaiser, and Gareth Morgan. "KLP38B: A Mitotic Kinesin-related Protein That Binds PP1." Journal of Cell Biology 138, no. 2 (July 28, 1997): 395–409. http://dx.doi.org/10.1083/jcb.138.2.395.

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We have identified a new member of the kinesin superfamily in Drosophila, KLP38B (kinesin-like protein at 38B). KLP38B was isolated through its two-hybrid interaction with the catalytic subunit of type 1 serine/threonine phosphoprotein phosphatase (PP1). We demonstrate that recombinant KLP38B and PP1 associate in vitro. This is the first demonstration of direct binding of a kinesin-related protein to a regulatory enzyme. Though most closely related to the Unc-104 subfamily of kinesin-related proteins, KLP38B is expressed only in proliferating cells. KLP38B mutants show cell proliferation defects in many tissues. KLP38B is required for normal chromatin condensation as embryos from KLP38B mutant mothers have undercondensed chromatin at metaphase and anaphase. This is the first time that a kinesin-related protein has been shown to have such a role. Incomplete lethality of a strong KLP38B allele suggests partial redundancy with one or more additional kinesin-related proteins.

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Mahase, Vidhyanand, Adebiyi Sobitan, Christina Johnson, Farion Cooper, Yixin Xie, Lin Li, and Shaolei Teng. "Computational analysis of hereditary spastic paraplegia mutations in the kinesin motor domains of KIF1A and KIF5A." Journal of Theoretical and Computational Chemistry 19, no. 06 (August 5, 2020): 2041003. http://dx.doi.org/10.1142/s0219633620410035.

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Hereditary spastic paraplegias (HSPs) are a genetically heterogeneous collection of neurodegenerative disorders categorized by progressive lower-limb spasticity and frailty. The complex HSP forms are characterized by various neurological features including progressive spastic weakness, urinary sphincter dysfunction, extra pyramidal signs and intellectual disability (ID). The kinesin superfamily proteins (KIFs) are microtubule-dependent molecular motors involved in intracellular transport. Kinesins directionally transport membrane vesicles, protein complexes, and mRNAs along neurites, thus playing important roles in neuronal development and function. Recent genetic studies have identified kinesin mutations in patients with HSPs. In this study, we used the computational approaches to investigate the 40 missense mutations associated with HSP and ID in KIF1A and KIF5A. We performed homology modeling to construct the structures of kinesin–microtubule binding domain and kinesin–tubulin complex. We applied structure-based energy calculation methods to determine the effects of missense mutations on protein stability and protein–protein interaction. The results revealed that the most of disease-causing mutations could change the folding free energy of kinesin motor domain and the binding free energy of kinesin–tubulin complex. We found that E253K associated with ID in KIF1A decrease the protein stability of kinesin motor domains. We showed that the HSP mutations located in kinesin–tubulin complex interface, such as K253N and R280C in KIF5A, can destabilize the kinesin–tubulin complex. The computational analysis provides useful information for understanding the roles of kinesin mutations in the development of ID and HSPs.

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Okada, Y. "A Processive Single-Headed Motor: Kinesin Superfamily Protein KIF1A." Science 283, no. 5405 (February 19, 1999): 1152–57. http://dx.doi.org/10.1126/science.283.5405.1152.

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Cole, D. G., W. Z. Cande, R. J. Baskin, D. A. Skoufias, C. J. Hogan, and J. M. Scholey. "Isolation of a sea urchin egg kinesin-related protein using peptide antibodies." Journal of Cell Science 101, no. 2 (February 1, 1992): 291–301. http://dx.doi.org/10.1242/jcs.101.2.291.

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To understand the roles of kinesin and its relatives in cell division, it is necessary to identify and characterize multiple members of the kinesin superfamily from mitotic cells. To this end we have raised antisera to peptides corresponding to highly conserved regions of the motor domains of several known members of the kinesin superfamily. These peptide antibodies react specifically with the motor domains of kinesin and ncd protein, as expected, and they also react with several polypeptides (including kinesin heavy chain) that cosediment with microtubules (MTs) precipitated from AMPPNP-treated sea urchin egg cytosol. Subsequent fractionation of ATP eluates of these MTs yields a protein of relative molecular mass 330 × 10(3) that behaves as a complex of three polypeptides that are distinct from conventional kinesin subunits or fragments thereof. This complex contains 85 kDa and 95 kDa polypeptides, which react with our peptide antibodies, and a 115 kDa polypeptide, which does not. This triplet of polypeptides, which we refer to as KRP(85/95), binds to purified sea urchin egg tubulin in an AMPPNP-enhanced, ATP-sensitive manner and induces the formation of microtubule bundles. We therefore propose that the triplet corresponds to a novel sea urchin egg kinesin-related protein.

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Pereira, Andrea J., Brian Dalby, Russell J. Stewart, Stephen J. Doxsey, and Lawrence S. B. Goldstein. "Mitochondrial Association of a Plus End–Directed Microtubule Motor Expressed during Mitosis in Drosophila." Journal of Cell Biology 136, no. 5 (March 10, 1997): 1081–90. http://dx.doi.org/10.1083/jcb.136.5.1081.

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The kinesin superfamily is a large group of proteins (kinesin-like proteins [KLPs]) that share sequence similarity with the microtubule (MT) motor kinesin. Several members of this superfamily have been implicated in various stages of mitosis and meiosis. Here we report our studies on KLP67A of Drosophila. DNA sequence analysis of KLP67A predicts an MT motor protein with an amino-terminal motor domain. To prove this directly, KLP67A expressed in Escherichia coli was shown in an in vitro motility assay to move MTs in the plus direction. We also report expression analyses at both the mRNA and protein level, which implicate KLP67A in the localization of mitochondria in undifferentiated cell types. In situ hybridization studies of the KLP67A mRNA during embryogenesis and larval central nervous system development indicate a proliferation-specific expression pattern. Furthermore, when affinity-purified anti-KLP67A antisera are used to stain blastoderm embryos, mitochondria in the region of the spindle asters are labeled. These data suggest that KLP67A is a mitotic motor of Drosophila that may have the unique role of positioning mitochondria near the spindle.

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Tan, Dongyan, Ana B. Asenjo, Vito Mennella, David J. Sharp, and Hernando Sosa. "Kinesin-13s form rings around microtubules." Journal of Cell Biology 175, no. 1 (October 2, 2006): 25–31. http://dx.doi.org/10.1083/jcb.200605194.

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Kinesin is a superfamily of motor proteins that uses the energy of adenosine triphosphate hydrolysis to move and generate force along microtubules. A notable exception to this general description is found in the kinesin-13 family that actively depolymerizes microtubules rather than actively moving along them. This depolymerization activity is important in mitosis during chromosome segregation. It is still not fully clear by which mechanism kinesin-13s depolymerize microtubules. To address this issue, we used electron microscopy to investigate the interaction of kinesin-13s with microtubules. Surprisingly, we found that proteins of the kinesin-13 family form rings and spirals around microtubules. This is the first report of this type of oligomeric structure for any kinesin protein. These rings may allow kinesin-13s to stay at the ends of microtubules during depolymerization.

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Mi LEE, Young, and Wankee KIM. "Association of human kinesin superfamily protein member 4 with BRCA2-associated factor 35." Biochemical Journal 374, no. 2 (September 1, 2003): 497–503. http://dx.doi.org/10.1042/bj20030452.

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A large portion of human kinesin superfamily protein member 4 (KIF4) is associated with the nuclear matrix during the interphase, while a small portion is found in the cytoplasm. During mitosis, it is associated with chromosomes throughout the entire process. In the present study, we identified a protein that interacts with KIF4 using a yeast two-hybrid system, co-immunoprecipitation and co-fractionation. This protein is BRCA2-associated factor 35 (BRAF35) containing a non-specific DNA binding high-mobility-group domain and a kinesin-like coiled-coil domain. It appeared that the interaction between the two proteins occurs through their respective α-helical coiled-coil domains. The co-fractionation experiment revealed that KIF4 and BRAF35 were present in a complex of approx. 540 kDa. The composition and biological significance of this complex should be studied further.

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Hirokawa, Nobutaka, and Yasuko Noda. "Intracellular Transport and Kinesin Superfamily Proteins, KIFs: Structure, Function, and Dynamics." Physiological Reviews 88, no. 3 (July 2008): 1089–118. http://dx.doi.org/10.1152/physrev.00023.2007.

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Various molecular cell biology and molecular genetic approaches have indicated significant roles for kinesin superfamily proteins (KIFs) in intracellular transport and have shown that they are critical for cellular morphogenesis, functioning, and survival. KIFs not only transport various membrane organelles, protein complexes, and mRNAs for the maintenance of basic cellular activity, but also play significant roles for various mechanisms fundamental for life, such as brain wiring, higher brain functions such as memory and learning and activity-dependent neuronal survival during brain development, and for the determination of important developmental processes such as left-right asymmetry formation and suppression of tumorigenesis. Accumulating data have revealed a molecular mechanism of cargo recognition involving scaffolding or adaptor protein complexes. Intramolecular folding and phosphorylation also regulate the binding activity of motor proteins. New techniques using molecular biophysics, cryoelectron microscopy, and X-ray crystallography have detected structural changes in motor proteins, synchronized with ATP hydrolysis cycles, leading to the development of independent models of monomer and dimer motors for processive movement along microtubules.

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Seog, Dae-Hyun, and Jin Han. "Sorting Nexin 17 Interacts Directly with Kinesin Superfamily KIF1Bβ Protein." Korean Journal of Physiology and Pharmacology 12, no. 4 (2008): 199. http://dx.doi.org/10.4196/kjpp.2008.12.4.199.

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Miki, H., M. Setou, K. Kaneshiro, and N. Hirokawa. "All kinesin superfamily protein, KIF, genes in mouse and human." Proceedings of the National Academy of Sciences 98, no. 13 (June 19, 2001): 7004–11. http://dx.doi.org/10.1073/pnas.111145398.

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Bernstein, M., P. L. Beech, S. G. Katz, and J. L. Rosenbaum. "A new kinesin-like protein (Klp1) localized to a single microtubule of the Chlamydomonas flagellum." Journal of Cell Biology 125, no. 6 (June 15, 1994): 1313–26. http://dx.doi.org/10.1083/jcb.125.6.1313.

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The kinesin superfamily of mechanochemical proteins has been implicated in a wide variety of cellular processes. We have begun studies of kinesins in the unicellular biflagellate alga, Chlamydomonas reinhardtii. A full-length cDNA, KLP1, has been cloned and sequenced, and found to encode a new member of the kinesin superfamily. An antibody was raised against the nonconserved tail region of the Klp1 protein, and it was used to probe for Klp1 in extracts of isolated flagella and in situ. Immunofluorescence of whole cells indicated that Klp1 was present in both the flagella and cell bodies. In wild-type flagella, Klp1 was found tightly to the axoneme; immunogold labeling of wild-type axonemal whole mounts showed that Klp1 was restricted to one of the two central pair microtubules at the core of the axoneme. Klp1 was absent from the flagella of mutants lacking the central pair microtubules, but was present in mutant flagella from pf16 cells, which contain an unstable C1 microtubule, indicating that Klp1 was bound to the C2 central pair microtubule. Localization of Klp1 to the C2 microtubule was confirmed by immunogold labeling of negatively stained and thin-sectioned axonemes. These findings suggest that Klp1 may play a role in rotation or twisting of the central pair microtubules.

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Liu, Wenjuan, Chunlin Xu, Qingyang Meng, and Peng Kang. "The clinical value of kinesin superfamily protein 2A in hepatocellular carcinoma." Clinics and Research in Hepatology and Gastroenterology 45, no. 4 (July 2021): 101527. http://dx.doi.org/10.1016/j.clinre.2020.08.005.

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Walczak, Claire E., Hailing Zong, Sachin Jain, and Jane R. Stout. "Spatial regulation of astral microtubule dynamics by Kif18B in PtK cells." Molecular Biology of the Cell 27, no. 20 (October 15, 2016): 3021–30. http://dx.doi.org/10.1091/mbc.e16-04-0254.

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The spatial and temporal control of microtubule dynamics is fundamentally important for proper spindle assembly and chromosome segregation. This is achieved, in part, by the multitude of proteins that bind to and regulate spindle microtubules, including kinesin superfamily members, which act as microtubule-destabilizing enzymes. These fall into two general classes: the kinesin-13 proteins, which directly depolymerize microtubules, and the kinesin-8 proteins, which are plus end–directed motors that either destabilize microtubules or cap the microtubule plus ends. Here we analyze the contribution of a PtK kinesin-8 protein, Kif18B, in the control of mitotic microtubule dynamics. Knockdown of Kif18B causes defects in spindle microtubule organization and a dramatic increase in astral microtubules. Kif18B-knockdown cells had defects in chromosome alignment, but there were no defects in chromosome segregation. The long astral microtubules that occur in the absence of Kif18B are limited in length by the cell cortex. Using EB1 tracking, we show that Kif18B activity is spatially controlled, as loss of Kif18B has the most dramatic effect on the lifetimes of astral microtubules that extend toward the cell cortex. Together our studies provide new insight into how diverse kinesins contribute to spatial microtubule organization in the spindle.

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Wickstead, Bill, and Keith Gull. "A “Holistic” Kinesin Phylogeny Reveals New Kinesin Families and Predicts Protein Functions." Molecular Biology of the Cell 17, no. 4 (April 2006): 1734–43. http://dx.doi.org/10.1091/mbc.e05-11-1090.

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Kinesin superfamily proteins are ubiquitous to all eukaryotes and essential for several key cellular processes. With the establishment of genome sequence data for a substantial number of eukaryotes, it is now possible for the first time to analyze the complete kinesin repertoires of a diversity of organisms from most eukaryotic kingdoms. Such a “holistic” approach using 486 kinesin-like sequences from 19 eukaryotes and analyzed by Bayesian techniques, identifies three new kinesin families, two new phylum-specific groups, and unites two previously identified families. The paralogue distribution suggests that the eukaryotic cenancestor possessed nearly all kinesin families. However, multiple losses in individual lineages mean that no family is ubiquitous to all organisms and that the present day distribution reflects common biology more than it does common ancestry. In particular, the distribution of four families—Kinesin-2, -9, and the proposed new families Kinesin-16 and -17—correlates with the possession of cilia/flagella, and this can be used to predict a flagellar function for two new kinesin families. Finally, we present a set of hidden Markov models that can reliably place most new kinesin sequences into families, even when from an organism at a great evolutionary distance from those in the analysis.

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Maor-Nof, Maya, Noriko Homma, Calanit Raanan, Aviv Nof, Nobutaka Hirokawa, and Avraham Yaron. "Axonal Pruning Is Actively Regulated by the Microtubule-Destabilizing Protein Kinesin Superfamily Protein 2A." Cell Reports 3, no. 4 (April 2013): 971–77. http://dx.doi.org/10.1016/j.celrep.2013.03.005.

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Kim, Wankee, Yao Tang, Yasushi Okada, Ted A. Torrey, Sisir K. Chattopadhyay, Michael Pfleiderer, Falko G. Falkner, et al. "Binding of Murine Leukemia Virus Gag Polyproteins to KIF4, a Microtubule-Based Motor Protein." Journal of Virology 72, no. 8 (August 1, 1998): 6898–901. http://dx.doi.org/10.1128/jvi.72.8.6898-6901.1998.

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ABSTRACT A cDNA clone encoding a cellular protein that interacts with murine leukemia virus (MuLV) Gag proteins was isolated from a T-cell lymphoma library. The sequence of the clone is identical to the C terminus of a cellular protein, KIF4, a microtubule-associated motor protein that belongs to the kinesin superfamily. KIF4-MuLV Gag associations have been detected in vitro and in vivo in mammalian cells. We suggest that KIF4 could be involved in Gag polyprotein translocation from the cytoplasm to the cell membrane.

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Wein, H., M. Foss, B. Brady, and W. Z. Cande. "DSK1, a novel kinesin-related protein from the diatom Cylindrotheca fusiformis that is involved in anaphase spindle elongation." Journal of Cell Biology 133, no. 3 (May 1, 1996): 595–604. http://dx.doi.org/10.1083/jcb.133.3.595.

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We have identified an 80-kD protein that is involved in mitotic spindle elongation in the diatom Cylindrotheca fusiformis. DSK1 (Diatom Spindle Kinesin 1) was isolated using a peptide antibody raised against a conserved region in the motor domain of the kinesin superfamily. By sequence homology, DSK1 belongs to the central motor family of kinesin-related proteins. Immunoblots using an antibody raised against a non-conserved region of DSK1 show that DSK1 is greatly enriched in mitotic spindle preparations. Anti-DSK1 stains in diatom central spindle with a bias toward the midzone, and staining is retained in the spindle midzone during spindle elongation in vitro. Furthermore, preincubation with anti-DSK1 blocks function in an in vitro spindle elongation assay. This inhibition of spindle elongation can be rescued by preincubating concurrently with the fusion protein against which anti-DSK1 was raised. We conclude that DSK1 is involved in spindle elongation and is likely to be responsible for pushing hal-spindles apart in the spindle midzone.

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Homma, Noriko, Yosuke Takei, Yosuke Tanaka, Takao Nakata, Sumio Terada, Masahide Kikkawa, Yasuko Noda, and Nobutaka Hirokawa. "Kinesin Superfamily Protein 2A (KIF2A) Functions in Suppression of Collateral Branch Extension." Cell 114, no. 2 (July 2003): 229–39. http://dx.doi.org/10.1016/s0092-8674(03)00522-1.

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Vukajlovic, Marija, Hendrik Dietz, Manfred Schliwa, and Zeynep Ökten. "How kinesin-2 forms a stalk." Molecular Biology of the Cell 22, no. 22 (November 15, 2011): 4279–87. http://dx.doi.org/10.1091/mbc.e11-02-0112.

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The heterotrimeric structure of kinesin-2 makes it a unique member of the kinesin superfamily; however, molecular details of the oligomer formation are largely unknown. Here we demonstrate that heterodimerization of the two distinct motor domains KLP11 and KLP20 of Caenorhabditis elegans kinesin-2 requires a dimerization seed of merely two heptads at the C terminus of the stalk. This heterodimeric seed is sufficient to promote dimerization along the entire length of the stalk, as shown by circular dichroism spectroscopy, Förster resonance energy transfer analysis, and electron microscopy. In addition to explaining the formation of the kinesin-2 stalk, the seed sequence identified here bears great potential for generating specific heterodimerization in other protein biochemical applications.

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Ye, Zhaoshun, Zhen Yuan, Huan Xu, Leiwen Pan, Jingsi Chen, Anicet Gatera, Muhammad Uzair, and Dawei Xu. "Genome-Wide Identification and Expression Analysis of Kinesin Family in Barley (Hordeum vulgare)." Genes 13, no. 12 (December 16, 2022): 2376. http://dx.doi.org/10.3390/genes13122376.

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Kinesin, as a member of the molecular motor protein superfamily, plays an essential function in various plants’ developmental processes. Especially at the early stages of plant growth, including influences on plants’ growth rate, yield, and quality. In this study, we did a genome-wide identification and expression profile analysis of the kinesin family in barley. Forty-two HvKINs were identified and screened from the barley genome, and a generated phylogenetic tree was used to compare the evolutionary relationships between Rice and Arabidopsis. The protein structure prediction, physicochemical properties, and bioinformatics of the HvKINs were also dissected. Our results reveal the important regulatory roles of HvKIN genes in barley growth. We found many cis- elements related to GA3 and ABA in homeopathic elements of the HvKIN gene and verified them by QRT-PCR, indicating their potential role in the barley kinesin family. The current study revealed the biological functions of barley kinesin genes in barley and will aid in further investigating the kinesin in other plant species.

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Williams, B. C., M. F. Riedy, E. V. Williams, M. Gatti, and M. L. Goldberg. "The Drosophila kinesin-like protein KLP3A is a midbody component required for central spindle assembly and initiation of cytokinesis." Journal of Cell Biology 129, no. 3 (May 1, 1995): 709–23. http://dx.doi.org/10.1083/jcb.129.3.709.

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We describe here a new member of the kinesin superfamily in Drosophila, KLP3A (Kinesin-Like-Protein-at-3A). The KLP3A protein localizes to the equator of the central spindle during late anaphase and telophase of male meiosis. Mutations in the KLP3A gene disrupt the interdigitation of microtubules in spermatocyte central spindles. Despite this defect, anaphase B spindle elongation is not obviously aberrant. However, cytokinesis frequently fails after both meiotic divisions in mutant testes. Together, these findings strongly suggest that the KLP3A presumptive motor protein is a critical component in the establishment or stabilization of the central spindle. Furthermore, these results imply that the central spindle is the source of signals that initiate the cleavage furrow in higher cells.

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Karuna, Edith, Shannon Choi, Michael Scales, Jennie Hum, Michael Cohen, Fernando Fierro, and Hsin-Yi Ho. "Identification of a WNT5A-Responsive Degradation Domain in the Kinesin Superfamily Protein KIF26B." Genes 9, no. 4 (April 5, 2018): 196. http://dx.doi.org/10.3390/genes9040196.

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Niwa, Shinsuke, Ruyung Zhou, Noriko Homma, Yosuke Takei, and Nobutaka Hirokawa. "Regulation of enteric nervous system development by a novel Kinesin superfamily protein KIF26A." Neuroscience Research 68 (January 2010): e124-e125. http://dx.doi.org/10.1016/j.neures.2010.07.2122.

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Oh, Sejo, Hwasun Hahn, Ted A. Torrey, Hyunjin Shin, Wonja Choi, Young Mi Lee, Herbert C. Morse, and Wankee Kim. "Identification of the human homologue of mouse KIF4, a kinesin superfamily motor protein." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1493, no. 1-2 (September 2000): 219–24. http://dx.doi.org/10.1016/s0167-4781(00)00151-2.

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Gao, Yang, Hui Zheng, Liangdong Li, Changshuai Zhou, Xin Chen, Xiaoyan Zhou, and Yiqun Cao. "KIF3C Promotes Proliferation, Migration, and Invasion of Glioma Cells by Activating the PI3K/AKT Pathway and Inducing EMT." BioMed Research International 2020 (October 22, 2020): 1–10. http://dx.doi.org/10.1155/2020/6349312.

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Kinesin superfamily protein 3C (KIF3C), a motor protein of the kinesin superfamily, is expressed in the central nervous system (CNS). Recently, several studies have suggested that KIF3C may act as a potential therapeutic target in solid tumors. However, the exact function and possible mechanism of the motor protein KIF3C in glioma remain unclear. In this study, a variety of tests including CCK-8, migration, invasion, and flow cytometry assays, and western blot were conducted to explore the role of KIF3C in glioma cell lines (U87 and U251). We found that overexpression of KIF3C in glioma cell lines promoted cell proliferation, migration, and invasion and suppressed apoptosis, while silencing of KIF3C reversed these effects. Ectopic KIF3C also increased the expression of N-cadherin, vimentin, snail, and slug to promote the epithelial-mesenchymal transition (EMT). Mechanistically, overexpression of KIF3C increased the levels of phosphatidylinositol 3-kinase (PI3K) and phosphorylated protein kinase B (p-AKT). These responses were reversed by KIF3C downregulation or AKT inhibition. Our results indicate that KIF3C promotes proliferation, migration, and invasion and inhibits apoptosis in glioma cells, possibly by activating the PI3K/AKT pathway in vitro. KIF3C might act as a potential biomarker or therapeutic target for further basic research or clinical management of glioma.

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Hogan, C. J., L. Stephens, T. Shimizu, and W. Z. Cande. "Physiological evidence for involvement of a kinesin-related protein during anaphase spindle elongation in diatom central spindles." Journal of Cell Biology 119, no. 5 (December 1, 1992): 1277–86. http://dx.doi.org/10.1083/jcb.119.5.1277.

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We have developed a new model system for studying spindle elongation in vitro using the pennate, marine diatom Cylindrotheca fusiformis. C. fusiformis can be grown in bulk to high densities while in log phase growth and synchronized by a simple light/dark regime. Isolated spindles can be attained in quantities sufficient for biochemical analysis and spindle tubulin is approximately 5% of the total protein present. The spindle isolation procedure results in a 10-fold enrichment of diatom tubulin and a calculated 40-fold increase in spindle protein. Isolated spindles or spindles in permeabilized cells can elongate in vitro by the same mechanism and with the same pharmacological sensitivities as described for other anaphase B models (Cande and McDonald, 1986; Masuda et al., 1990). Using this model, in vitro spindle elongation rate profiles were developed for a battery of nucleotide triphosphates and ATP analogs. The relative rates of spindle elongation produced by various nucleotide triphosphates parallel relative rates seen for kinesin-based motility in microtubule gliding assays. Likewise ATP analogs that allow discrimination between myosin-, dynein-, and kinesin-mediated motility produce relative spindle elongation rates characteristic of kinesin motility. Also, isolated spindle fractions are enriched for a kinesin related protein as identified by a peptide antibody against a conserved region of the kinesin superfamily. These data suggest that kinesin-like motility contributes to spindle elongation during anaphase B of mitosis.

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Li, Guoqiang, Jianliang Chen, Shu Li, Shu Zhou, Shouji Cao, Yun Lou, Haiyuan Shen, and Jie Yin. "Kinesin superfamily protein expression and its association with progression and prognosis in hepatocellular carcinoma." Journal of Cancer Research and Therapeutics 13, no. 4 (2017): 651. http://dx.doi.org/10.4103/jcrt.jcrt_491_17.

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Takeda, Sen, Hiroto Yamazaki, Dae-Hyun Seog, Yoshimitsu Kanai, Sumio Terada, and Nobutaka Hirokawa. "Kinesin Superfamily Protein 3 (Kif3) Motor Transports Fodrin-Associating Vesicles Important for Neurite Building." Journal of Cell Biology 148, no. 6 (March 20, 2000): 1255–66. http://dx.doi.org/10.1083/jcb.148.6.1255.

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Kinesin superfamily proteins (KIFs) comprise several dozen molecular motor proteins. The KIF3 heterotrimer complex is one of the most abundantly and ubiquitously expressed KIFs in mammalian cells. To unveil the functions of KIF3, microinjection of function-blocking monovalent antibodies against KIF3 into cultured superior cervical ganglion (SCG) neurons was carried out. They significantly blocked fast axonal transport and brought about inhibition of neurite extension. A yeast two-hybrid binding assay revealed the association of fodrin with the KIF3 motor through KAP3. This was further confirmed by using vesicles collected from large bundles of axons (cauda equina), from which membranous vesicles could be prepared in pure preparations. Both immunoprecipitation and immunoelectron microscopy indicated the colocalization of fodrin and KIF3 on the same vesicles, the results reinforcing the evidence that the cargo of the KIF3 motor consists of fodrin-associating vesicles. In addition, pulse-labeling study implied partial comigration of both molecules as fast flow components. Taken together, the KIF3 motor is engaged in fast axonal transport that conveys membranous components important for neurite extension.

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Yamazaki, H., T. Nakata, Y. Okada, and N. Hirokawa. "Cloning and characterization of KAP3: a novel kinesin superfamily-associated protein of KIF3A/3B." Proceedings of the National Academy of Sciences 93, no. 16 (August 6, 1996): 8443–48. http://dx.doi.org/10.1073/pnas.93.16.8443.

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Setou, M. "Kinesin Superfamily Motor Protein KIF17 and mLin-10 in NMDA Receptor-Containing Vesicle Transport." Science 288, no. 5472 (June 9, 2000): 1796–802. http://dx.doi.org/10.1126/science.288.5472.1796.

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Walther, Z., M. Vashishtha, and J. L. Hall. "The Chlamydomonas FLA10 gene encodes a novel kinesin-homologous protein." Journal of Cell Biology 126, no. 1 (July 1, 1994): 175–88. http://dx.doi.org/10.1083/jcb.126.1.175.

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Many genes on the uni linkage group of Chlamydomonas affect the basal body/flagellar apparatus. Among these are five FLA genes, whose mutations cause temperature-sensitive defects in flagellar assembly. We present the molecular analysis of a gene which maps to fla10 and functionally rescues the fla10 phenotype. Nucleotide sequencing revealed that the gene encodes a kinesin-homologous protein, KHP1. The 87-kD predicted KHP1 protein, like kinesin heavy chain, has an amino-terminal motor domain, a central alpha-helical stalk, and a basic, globular carboxy-terminal tail. Comparison to other kinesin superfamily members indicated striking similarity (64% identity in motor domains) to a mouse gene, KIF3, expressed primarily in cerebellum. In synchronized cultures, the KHP1 mRNA accumulated after cell division, as did flagellar dynein mRNAs. KHP1 mRNA levels also increased following deflagellation. Polyclonal antibodies detected KHP1 protein in Western blots of purified flagella and axonemes. The protein was partially released from axonemes with ATP treatment, but not with AMP-PNP. Western blot analysis of axonemes from various motility mutants suggested that KHP1 is not a component of radial spokes, dynein arms, or the central pair complex. The quantity of KHP1 protein in axonemes of the mutant fla10-1 was markedly reduced, although no reduction was observed in two other uni linkage group mutants, fla9 and fla11. Furthermore, fla10-1 was rescued by transformation with KHP1 genomic DNA. These results indicate that KHP1 is the gene product of FLA10 and suggest a novel role for this kinesin-related protein in flagellar assembly and maintenance.

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Yang, Zhaohuai, Chun-hong Xia, Elizabeth A. Roberts, Kevin Bush, Sanjay K. Nigam, and Lawrence S. B. Goldstein. "Molecular Cloning and Functional Analysis of Mouse C-Terminal Kinesin Motor KifC3." Molecular and Cellular Biology 21, no. 3 (February 1, 2001): 765–70. http://dx.doi.org/10.1128/mcb.21.3.765-770.2001.

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ABSTRACT Proteins of the kinesin superfamily define a class of microtubule-dependent motors that play crucial roles in cell division and intracellular transport. To study the molecular mechanism of intracellular transport involving microtubule-dependent motors, a cDNA encoding a new kinesin-like protein called KifC3 was cloned from a mouse brain cDNA library. Sequence and secondary structure analysis revealed that KifC3 is a member of the C-terminal motor family. In contrast to other mouse C-terminal motors, KifC3 is apparently ubiquitous and may have a general role in intracellular transport. To understand the in vivo function of the KifC3 gene, we used homologous recombination in embryonic stem cells to construct knockout mouse strains for the KifC3 gene. Homozygous mutants of theKifC3 gene are viable, reproduce normally, and apparently develop normally. These results suggest that KifC3 is dispensable for normal development and reproduction in the mouse.

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Hares, Kelly, Scott Miners, Neil Scolding, Seth Love, and Alastair Wilkins. "KIF5A and KLC1 expression in Alzheimer’s disease: relationship and genetic influences." AMRC Open Research 1 (February 19, 2019): 1. http://dx.doi.org/10.12688/amrcopenres.12861.1.

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Background: Early disturbances in axonal transport, before the onset of gross neuropathology, occur in a spectrum of neurodegenerative diseases including Alzheimer’s disease. Kinesin superfamily motor proteins (KIFs) are responsible for anterograde protein transport within the axon of various cellular cargoes, including synaptic and structural proteins. Dysregulated KIF expression has been associated with AD pathology and genetic polymorphisms within kinesin-light chain-1 (KLC1) have been linked to AD susceptibility. We examined the expression of KLC1 in AD, in relation to that of the KLC1 motor complex (KIF5A) and to susceptibility genotypes. Methods: We analysed KLC1 and KIF5A gene and protein expression in midfrontal cortex from 47 AD and 39 control brains. Results: We found that gene expression of both KIF5A and KLC1 increased with Braak tangle stage (0-II vs III-IV and V-VI) but was not associated with significant change at the protein level. We found no effect of KLC1 SNPs on KIF5A or KLC1 expression but KIF5A SNPs that had previously been linked to susceptibility in multiple sclerosis were associated with reduced KIF5A mRNA expression in AD cortex. Conclusions: The findings raise the possibility that genetic polymorphisms within the KIF5A gene locus could contribute to disturbances of axonal transport, neuronal connectivity and function across a spectrum of neurological conditions, including AD.

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Sakurai, Shunya, Toshiyuki Shimizu, and Umeharu Ohto. "Crystal structure of the FYCO1 RUN domain suggests possible interfaces with small GTPases." Acta Crystallographica Section F Structural Biology Communications 76, no. 8 (July 28, 2020): 326–33. http://dx.doi.org/10.1107/s2053230x20009012.

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FYCO1 is a multidomain adaptor protein that plays an important role in autophagy by mediating the kinesin-dependent microtubule plus-end-directed transport of autophagosomes. FYCO1 contains a RUN domain, which is hypothesized to function as a specific effector for members of the Ras superfamily of small GTPases, but its role has not been well characterized and its interaction partner(s) have not been identified. Here, the crystal structure of the FYCO1 RUN domain was determined at 1.3 Å resolution. The overall structure of the FYCO1 RUN domain was similar to those of previously reported RUN domains. Detailed structural comparisons with other RUN domains and docking studies suggested a possible interaction interface of the FYCO1 RUN domain with small GTPases of the Ras superfamily.

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de Hostos, Eugenio L., Gretchen McCaffrey, Richard Sucgang, Daniel W. Pierce, and Ronald D. Vale. "A Developmentally Regulated Kinesin-related Motor Protein fromDictyostelium discoideum." Molecular Biology of the Cell 9, no. 8 (August 1998): 2093–106. http://dx.doi.org/10.1091/mbc.9.8.2093.

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The cellular slime mold Dictyostelium discoideum is an attractive system for studying the roles of microtubule-based motility in cell development and differentiation. In this work, we report the first molecular characterization of kinesin-related proteins (KRPs) in Dictyostelium. A PCR-based strategy was used to isolate DNA fragments encoding six KRPs, several of which are induced during the developmental program that is initiated by starvation. The complete sequence of one such developmentally regulated KRP (designated K7) was determined and found to be a novel member of the kinesin superfamily. The motor domain of K7 is most similar to that of conventional kinesin, but unlike conventional kinesin, K7 is not predicted to have an extensive α-helical coiled-coil domain. The nonmotor domain is unusual and is rich in Asn, Gln, and Thr residues; similar sequences are found in other developmentally regulated genes inDictyostelium. K7, expressed in Escherichia coli, supports plus end–directed microtubule motility in vitro at a speed of 0.14 μm/s, indicating that it is a bona fide motor protein. The K7 motor is found only in developing cells and reaches a peak level of expression between 12 and 16 h after starvation. By immunofluorescence microscopy, K7 localizes to a membranous perinuclear structure. To examine K7 function, we prepared a null cell line but found that these cells show no gross developmental abnormalities. However, when cultivated in the presence of wild-type cells, the K7-null cells are mostly absent from the prestalk zone of the slug. This result suggests that in a population composed largely of wild-type cells, the absence of the K7 motor protein interferes either with the ability of the cells to localize to the prestalk zone or to differentiate into prestalk cells.

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Okada, Y. "2SA01 Atomic model of depolymerization mechanism of micro-tubules by a kinesin superfamily protein, KIF2C." Seibutsu Butsuri 44, supplement (2004): S13. http://dx.doi.org/10.2142/biophys.44.s13_3.

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Lee, Young Mi, and Wankee Kim. "Kinesin superfamily protein member 4 (KIF4) is localized to midzone and midbody in dividing cells." Experimental & Molecular Medicine 36, no. 1 (February 2004): 93–97. http://dx.doi.org/10.1038/emm.2004.13.

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Noda, Y., R. Sato-Yoshitake, S. Kondo, M. Nangaku, and N. Hirokawa. "KIF2 is a new microtubule-based anterograde motor that transports membranous organelles distinct from those carried by kinesin heavy chain or KIF3A/B." Journal of Cell Biology 129, no. 1 (April 1, 1995): 157–67. http://dx.doi.org/10.1083/jcb.129.1.157.

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Kinesin is known as a representative cytoskeletal motor protein that is engaged in cell division and axonal transport. In addition to the mutant assay, recent advances using the PCR cloning technique have elucidated the existence of many kinds of kinesin-related proteins in yeast, Drosophila, and mice. We previously cloned five different members of kinesin superfamily proteins (KIFs) in mouse brain (Aizawa, H., Y. Sekine, R. Takemura, Z. Zhang, M. Nangaku, and N. Hirokawa. 1992. J. Cell Biol. 119:1287-1296) and demonstrated that one of them, KIF3A, is an anterograde motor (Kondo, S., R. Sato-Yashitake, Y. Noda, H. Aizawa, T. Nakata, Y. Matsuura, and N. Hirokawa. J. Cell Biol. 1994. 125:1095-1107). We have now characterized another axonal transport motor, KIF2. Different from other KIFs, KIF2 is a central type motor, since its motor domain is located in the center of the molecule. Recombinant KIF2 exists as a dimer with a bigger head and plus-end directionally moves microtubules at a velocity of 0.47 +/- 0.11 microns/s, which is two thirds that of kinesin's. Immunocytological examination showed that native KIF2 is abundant in developing axons and that it accumulates in the proximal region of the ligated nerves after a 20-h ligation. Soluble KIF2 exists without a light chain, and KIF2's associated-vesicles, immunoprecipitated by anti-KIF2 antibody, are different from those carried by existing motors such as kinesin and KIF3A. They are also distinct from synaptic vesicles, although KIF2 is accumulated in so-called synaptic vesicle fractions and embryonal growth cone particles. Our results strongly suggest that KIF2 functions as a new anterograde motor, being specialized for a particular group of membranous organelles involved in fast axonal transport.

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44

Mao, Cui, Xing Ju, Haijian Cheng, Xixia Huang, Fugui Jiang, Yuni Yao, Xianyong Lan, and Enliang Song. "Determination of genetic variation within the <i>DYRK2</i> gene and its associations with milk traits in cattle." Archives Animal Breeding 63, no. 2 (September 9, 2020): 315–23. http://dx.doi.org/10.5194/aab-63-315-2020.

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Abstract. To speed up the progress of marker-assisted selection (MAS) in cattle breeding, the dual-specificity tyrosine phosphorylation-regulated kinase 2 (DYRK2), cadherin 2 (CDH2), and kinesin family member 1A (KIF1A) genes were chosen based on our pervious genome-wide association study (GWAS) analysis results. DYRK2 is a kinase that may participate in cell growth and/or development; it shows phosphorylation activity toward serine, threonine, and tyrosine fragments of proteins, and it is different from other protein kinases. The CDH2 gene encodes a classic cadherin, which is a member of the cadherin superfamily. The protein encoded by KIF1A is a member of the kinesin family and plays a role in the transportation of membrane organelles along axon microtubules. We detected insertion/deletion (InDel) variation in these three candidate genes in 438 individual cattle (Xinjiang Brown cattle and Wagyu × Luxi crossbreed cattle). Only DYRK2-P3-11 bp was polymorphic and genotyped. The polymorphism information content of DYRK2-P3-11 bp was 0.336. Correlation analyses showed that InDel polymorphism was significantly associated with six different milk traits. These findings may aid future analyses of InDel genotypes in cattle breeds, and speed up the progress of MAS in cattle breeding.

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Hares, Kelly, Scott Miners, Neil Scolding, Seth Love, and Alastair Wilkins. "KIF5A and KLC1 expression in Alzheimer’s disease: relationship and genetic influences." AMRC Open Research 1 (June 26, 2019): 1. http://dx.doi.org/10.12688/amrcopenres.12861.2.

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Background: Early disturbances in axonal transport, before the onset of gross neuropathology, occur in a spectrum of neurodegenerative diseases including Alzheimer’s disease. Kinesin superfamily motor proteins (KIFs) are responsible for anterograde protein transport within the axon of various cellular cargoes, including synaptic and structural proteins. Dysregulated KIF expression has been associated with AD pathology and genetic polymorphisms within kinesin-light chain-1 (KLC1) have been linked to AD susceptibility. We examined the expression of KLC1 in AD, in relation to that of the KLC1 motor complex (KIF5A) and to susceptibility genotypes. Methods: We analysed KLC1 and KIF5A gene and protein expression in midfrontal cortex from 47 AD and 39 control brains. Results: We found that gene expression of both KIF5A and KLC1 increased with Braak tangle stage (0-II vs III-IV and V-VI) but was not associated with significant change at the protein level. We found no effect of KLC1 SNPs on KIF5A or KLC1 expression but KIF5A SNPs that had previously been linked to susceptibility in multiple sclerosis were associated with reduced KIF5A mRNA expression in AD cortex. Conclusions: Future in vitro and in vivo studies are required to understand the cause of upregulated KIF5A and KLC-1 gene expression in AD and any potential downstream consequences on pathogenesis, including any contribution of genetic polymorphisms within the KIF5A gene locus.

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Bernasconi, Pia, Cristina Cappelletti, Francesca Navone, Valeria Nessi, Fulvio Baggi, Isabelle Vernos, Stefania Romaggi, et al. "The Kinesin Superfamily Motor Protein KIF4 Is Associated With Immune Cell Activation in Idiopathic Inflammatory Myopathies." Journal of Neuropathology & Experimental Neurology 67, no. 6 (June 2008): 624–32. http://dx.doi.org/10.1097/nen.0b013e318177e5fd.

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Takeda, Sen, Yoshiaki Yonekawa, Yosuke Tanaka, Yasushi Okada, Shigenori Nonaka, and Nobutaka Hirokawa. "Left-Right Asymmetry and Kinesin Superfamily Protein KIF3A: New Insights in Determination of Laterality and Mesoderm Induction by kif3A−/− Mice Analysis." Journal of Cell Biology 145, no. 4 (May 17, 1999): 825–36. http://dx.doi.org/10.1083/jcb.145.4.825.

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KIF3A is a classical member of the kinesin superfamily proteins (KIFs), ubiquitously expressed although predominantly in neural tissues, and which forms a heterotrimeric KIF3 complex with KIF3B or KIF3C and an associated protein, KAP3. To elucidate the function of the kif3A gene in vivo, we made kif3A knockout mice. kif3A−/− embryos displayed severe developmental abnormalities characterized by neural tube degeneration and mesodermal and caudal dysgenesis and died during the midgestational period at ∼10.5 dpc (days post coitum), possibly resulting from cardiovascular insufficiency. Whole mount in situ hybridization of Pax6 revealed a normal pattern while staining by sonic hedgehog (shh) and Brachyury (T) exhibited abnormal patterns in the anterior-posterior (A-P) direction at both mesencephalic and thoracic levels. These results suggest that KIF3A might be involved in mesodermal patterning and in turn neurogenesis.

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Yamazaki, H., T. Nakata, Y. Okada, and N. Hirokawa. "KIF3A/B: a heterodimeric kinesin superfamily protein that works as a microtubule plus end-directed motor for membrane organelle transport." Journal of Cell Biology 130, no. 6 (September 15, 1995): 1387–99. http://dx.doi.org/10.1083/jcb.130.6.1387.

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We cloned a new member of the murine brain kinesin superfamily, KIF3B, and found that its amino acid sequence is highly homologous but not identical to KIF3A, which we previously cloned and named KIF3 (47% identical). KIF3B is localized in various organ tissues and developing neurons of mice and accumulates with anterogradely moving membranous organelles after ligation of nerve axons. Immunoprecipitation assay of the brain revealed that KIF3B forms a complex with KIF3A and three other high molecular weight (approximately 100 kD)-associated polypeptides, called the kinesin superfamily-associated protein 3 (KAP3). In vitro reconstruction using baculovirus expression systems showed that KIF3A and KIF3B directly bind with each other in the absence of KAP3. The recombinant KIF3A/B complex (approximately 50-nm rod with two globular heads and a single globular tail) demonstrated plus end-directed microtubule sliding activity in vitro. In addition, we showed that KIF3B itself has motor activity in vitro, by making a complex of wild-type KIF3B and a chimeric motor protein (KIF3B head and KIF3A rod tail). Subcellular fractionation of mouse brain homogenates showed a considerable amount of the native KIF3 complex to be associated with membrane fractions other than synaptic vesicles. Immunoprecipitation by anti-KIF3B antibody-conjugated beads and its electron microscopic study also revealed that KIF3 is associated with membranous organelles. Moreover, we found that the composition of KAP3 is different in the brain and testis. Our findings suggest that KIF3B forms a heterodimer with KIF3A and functions as a new microtubule-based anterograde translocator for membranous organelles, and that KAP3 may determine functional diversity of the KIF3 complex in various kinds of cells in vivo.

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Bunn, Robert C., Mari Anne Jensen, and Brent C. Reed. "Protein Interactions with the Glucose Transporter Binding Protein GLUT1CBP That Provide a Link between GLUT1 and the Cytoskeleton." Molecular Biology of the Cell 10, no. 4 (April 1999): 819–32. http://dx.doi.org/10.1091/mbc.10.4.819.

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Subcellular targeting and the activity of facilitative glucose transporters are likely to be regulated by interactions with cellular proteins. This report describes the identification and characterization of a protein, GLUT1 C-terminal binding protein (GLUT1CBP), that binds via a PDZ domain to the C terminus of GLUT1. The interaction requires the C-terminal four amino acids of GLUT1 and is isoform specific because GLUT1CBP does not interact with the C terminus of GLUT3 or GLUT4. Most rat tissues examined contain both GLUT1CBP and GLUT1 mRNA, whereas only small intestine lacked detectable GLUT1CBP protein. GLUT1CBP is also expressed in primary cultures of neurons and astrocytes, as well as in Chinese hamster ovary, 3T3-L1, Madin–Darby canine kidney, Caco-2, and pheochromocytoma-12 cell lines. GLUT1CBP is able to bind to native GLUT1 extracted from cell membranes, self-associate, or interact with the cytoskeletal proteins myosin VI, α-actinin-1, and the kinesin superfamily protein KIF-1B. The presence of a PDZ domain places GLUT1CBP among a growing family of structural and regulatory proteins, many of which are localized to areas of membrane specialization. This and its ability to interact with GLUT1 and cytoskeletal proteins implicate GLUT1CBP in cellular mechanisms for targeting GLUT1 to specific subcellular sites either by tethering the transporter to cytoskeletal motor proteins or by anchoring the transporter to the actin cytoskeleton.

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Yang, Zhaohuai, and Lawrence S. B. Goldstein. "Characterization of the KIF3C Neural Kinesin-like Motor from Mouse." Molecular Biology of the Cell 9, no. 2 (February 1998): 249–61. http://dx.doi.org/10.1091/mbc.9.2.249.

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Proteins of the kinesin superfamily define a class of microtubule-dependent motors that play crucial roles in cell division and intracellular transport. To study the molecular mechanism of axonal transport, a cDNA encoding a new kinesin-like protein called KIF3C was cloned from a mouse brain cDNA library. Sequence and secondary structure analysis revealed that KIF3C is a member of the KIF3 family. In contrast to KIF3A and KIF3B, Northern and Western analysis indicated that KIF3C expression is highly enriched in neural tissues such as brain, spinal cord, and retina. When anti-KIF3C antibodies were used to stain the cerebellum, the strongest signal came from the cell bodies and dendrites of Purkinje cells. In retina, anti-KIF3C mainly stains the ganglion cells. Immunolocalization showed that the KIF3C motor in spinal cord and sciatic nerve is mainly localized in cytoplasm. In spinal cord, the KIF3C staining was punctate; double labeling with anti-giantin and anti-KIF3C showed a clear concentration of the motor protein in the Golgi complex. Staining of ligated sciatic nerves demonstrated that the KIF3C motor accumulated at the proximal side of the ligated nerve, which suggests that KIF3C is an anterograde motor. Immunoprecipitation experiments revealed that KIF3C and KIF3A, but not KIF3B, were coprecipitated. These data, combined with previous data from other labs, indicate that KIF3C and KIF3B are “variable” subunits that associate with a common KIF3A subunit, but not with each other. Together these results suggest that KIF3 family members combinatorially associate to power anterograde axonal transport.

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Journal articles on the topic 'Kinesin superfamily protein'

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