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Gotowa bibliografia na temat „Retrograde protein 1”

Autor: Grafiati

Data publikacji: 6 września 2023

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Artykuły w czasopismach na temat "Retrograde protein 1"

1

Blacque, Oliver E., Chunmei Li, Peter N. Inglis, et al. "The WD Repeat-containing Protein IFTA-1 Is Required for Retrograde Intraflagellar Transport." Molecular Biology of the Cell 17, no. 12 (2006): 5053–62. http://dx.doi.org/10.1091/mbc.e06-06-0571.

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The assembly and maintenance of cilia require intraflagellar transport (IFT), a microtubule-dependent bidirectional motility of multisubunit protein complexes along ciliary axonemes. Defects in IFT and the functions of motile or sensory cilia are associated with numerous human ailments, including polycystic kidney disease and Bardet–Biedl syndrome. Here, we identify a novel Caenorhabditis elegans IFT gene, IFT-associated gene 1 (ifta-1), which encodes a WD repeat-containing protein with strong homology to a mammalian protein of unknown function. Both the C. elegans and human IFTA-1 proteins lo

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Schafer, Jenny C., Courtney J. Haycraft, James H. Thomas, Bradley K. Yoder, and Peter Swoboda. "XBX-1 Encodes a Dynein Light Intermediate Chain Required for Retrograde Intraflagellar Transport and Cilia Assembly in Caenorhabditis elegans." Molecular Biology of the Cell 14, no. 5 (2003): 2057–70. http://dx.doi.org/10.1091/mbc.e02-10-0677.

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Intraflagellar transport (IFT) is a process required for flagella and cilia assembly that describes the dynein and kinesin mediated movement of particles along axonemes that consists of an A and a B complex, defects in which disrupt retrograde and anterograde transport, respectively. Herein, we describe a novel Caenorhabditis elegans gene, xbx-1, that is required for retrograde IFT and shares homology with a mammalian dynein light intermediate chain (D2LIC). xbx-1 expression in ciliated sensory neurons is regulated by the transcription factor DAF-19, as demonstrated previously for genes encodi

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3

Anderson, Nadine S., Indrani Mukherjee, Christine M. Bentivoglio, and Charles Barlowe. "The golgin protein Coy1 functions in intra-Golgi retrograde transport and interacts with the COG complex and Golgi SNAREs." Molecular Biology of the Cell 28, no. 20 (2017): 2686–700. http://dx.doi.org/10.1091/mbc.e17-03-0137.

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Extended coiled-coil proteins of the golgin family play prominent roles in maintaining the structure and function of the Golgi complex. Here we further investigate the golgin protein Coy1 and document its function in retrograde transport between early Golgi compartments. Cells that lack Coy1 displayed a reduced half-life of the Och1 mannosyltransferase, an established cargo of intra-Golgi retrograde transport. Combining the coy1Δ mutation with deletions in other putative retrograde golgins (sgm1Δ and rud3Δ) caused strong glycosylation and growth defects and reduced membrane association of the

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4

Hollenbeck, P. J., and D. Bray. "Rapidly transported organelles containing membrane and cytoskeletal components: their relation to axonal growth." Journal of Cell Biology 105, no. 6 (1987): 2827–35. http://dx.doi.org/10.1083/jcb.105.6.2827.

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We have examined the movements, composition, and cellular origin of phase-dense varicosities in cultures of chick sympathetic and sensory neurons. These organelles are variable in diameter (typically between 0.2 and 2 microns) and undergo saltatory movements both towards and away from the neuronal cell body. Their mean velocities vary inversely with the size of the organelle and are greater in the retrograde than the anterograde direction. Organelles stain with the lipophilic dye 1, 1'-dioctadecyl-3,3,3',3'-tetramethyl-indocarbocyanine and with antibodies to cytoskeletal components. In culture

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5

Buser, Dominik P., Kai D. Schleicher, Cristina Prescianotto-Baschong, and Martin Spiess. "A versatile nanobody-based toolkit to analyze retrograde transport from the cell surface." Proceedings of the National Academy of Sciences 115, no. 27 (2018): E6227—E6236. http://dx.doi.org/10.1073/pnas.1801865115.

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Retrograde transport of membranes and proteins from the cell surface to the Golgi and beyond is essential to maintain homeostasis, compartment identity, and physiological functions. To study retrograde traffic biochemically, by live-cell imaging or by electron microscopy, we engineered functionalized anti-GFP nanobodies (camelid VHH antibody domains) to be bacterially expressed and purified. Tyrosine sulfation consensus sequences were fused to the nanobody for biochemical detection of trans-Golgi arrival, fluorophores for fluorescence microscopy and live imaging, and APEX2 (ascorbate peroxidas

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6

Shimizu, Takayuki, Sylwia M. Kacprzak, Nobuyoshi Mochizuki, et al. "The retrograde signaling protein GUN1 regulates tetrapyrrole biosynthesis." Proceedings of the National Academy of Sciences 116, no. 49 (2019): 24900–24906. http://dx.doi.org/10.1073/pnas.1911251116.

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The biogenesis of the photosynthetic apparatus in developing seedlings requires the assembly of proteins encoded on both nuclear and chloroplast genomes. To coordinate this process there needs to be communication between these organelles, but the retrograde signals by which the chloroplast communicates with the nucleus at this time are still essentially unknown. The Arabidopsis thaliana genomes uncoupled (gun) mutants, that show elevated nuclear gene expression after chloroplast damage, have formed the basis of our understanding of retrograde signaling. Of the 6 reported gun mutations, 5 are i

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7

Signor, Dawn, Karen P. Wedaman, Jose T. Orozco, et al. "Role of a Class Dhc1b Dynein in Retrograde Transport of Ift Motors and Ift Raft Particles along Cilia, but Not Dendrites, in Chemosensory Neurons of Living Caenorhabditis elegans." Journal of Cell Biology 147, no. 3 (1999): 519–30. http://dx.doi.org/10.1083/jcb.147.3.519.

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The heterotrimeric motor protein, kinesin-II, and its presumptive cargo, can be observed moving anterogradely at 0.7 μm/s by intraflagellar transport (IFT) within sensory cilia of chemosensory neurons of living Caenorhabditis elegans, using a fluorescence microscope–based transport assay (Orozco, J.T., K.P. Wedaman, D. Signor, H. Brown, L. Rose, and J.M. Scholey. 1999. Nature. 398:674). Here, we report that kinesin-II, and two of its presumptive cargo molecules, OSM-1 and OSM-6, all move at ∼1.1 μm/s in the retrograde direction along cilia and dendrites, which is consistent with the hypothesis

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8

Cavolo, Samantha L., Chaoming Zhou, Stephanie A. Ketcham, et al. "Mycalolide B dissociates dynactin and abolishes retrograde axonal transport of dense-core vesicles." Molecular Biology of the Cell 26, no. 14 (2015): 2664–72. http://dx.doi.org/10.1091/mbc.e14-11-1564.

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Axonal transport is critical for maintaining synaptic transmission. Of interest, anterograde and retrograde axonal transport appear to be interdependent, as perturbing one directional motor often impairs movement in the opposite direction. Here live imaging of Drosophila and hippocampal neuron dense-core vesicles (DCVs) containing a neuropeptide or brain-derived neurotrophic factor shows that the F-actin depolymerizing macrolide toxin mycalolide B (MB) rapidly and selectively abolishes retrograde, but not anterograde, transport in the axon and the nerve terminal. Latrunculin A does not mimic M

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9

Ramos-García, Silvia L., Robert W. Roberson, Michael Freitag, Salomón Bartnicki-García, and Rosa R. Mouriño-Pérez. "Cytoplasmic Bulk Flow Propels Nuclei in Mature Hyphae of Neurospora crassa." Eukaryotic Cell 8, no. 12 (2009): 1880–90. http://dx.doi.org/10.1128/ec.00062-09.

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ABSTRACT We used confocal microscopy to evaluate nuclear dynamics in mature, growing hyphae of Neurospora crassa whose nuclei expressed histone H1-tagged green fluorescent protein (GFP). In addition to the H1-GFP wild-type (WT) strain, we examined nuclear displacement (passive transport) in four mutants deficient in microtubule-related motor proteins (ro-1, ro-3, kin-1, and a ro-1 kin-1 double mutant). We also treated the WT strain with benomyl and cytochalasin A to disrupt microtubules and actin microfilaments, respectively. We found that the degree of nuclear displacement in the subapical re

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10

Giannotta, Monica, Giorgia Fragassi, Antonio Tamburro, Capone Vanessa, Alberto Luini, and Michele Sallese. "Prohibitin: A Novel Molecular Player in KDEL Receptor Signalling." BioMed Research International 2015 (2015): 1–13. http://dx.doi.org/10.1155/2015/319454.

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The KDEL receptor (KDELR) is a seven-transmembrane-domain protein involved in retrograde transport of protein chaperones from the Golgi complex to the endoplasmic reticulum. Our recent findings have shown that the Golgi-localised KDELR acts as a functional G-protein-coupled receptor by binding to and activating Gs and Gq. These G proteins induce activation of PKA and Src and regulate retrograde and anterograde Golgi trafficking. Here we used an integrated coimmunoprecipitation and mass spectrometry approach to identify prohibitin-1 (PHB) as a KDELR interactor. PHB is a multifunctional protein

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