Journal articles: 'Hook domain'

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Xu, Lai, Mathew E. Sowa, Jing Chen, Xue Li, Steven P. Gygi, and J. Wade Harper. "An FTS/Hook/p107FHIP Complex Interacts with and Promotes Endosomal Clustering by the Homotypic Vacuolar Protein Sorting Complex." Molecular Biology of the Cell 19, no. 12 (December 2008): 5059–71. http://dx.doi.org/10.1091/mbc.e08-05-0473.

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Fused Toes (FTS) is a member of a small group of inactive variant E2 ubiquitin-conjugating enzyme domain-containing proteins of unknown function. Through proteomic analysis of FTS complexes purified from human embryonic kidney 293T cells, we identified a new multiprotein complex, the FHF complex, containing FTS, members of the microtubule-binding Hook family of coiled-coil proteins (Hook1, Hook2, and Hook3), and a previously uncharacterized 107-kDa protein, FTS and Hook Interacting Protein (FHIP). FTS associated with a conserved C-terminal motif in Hook proteins in the yeast two-hybrid system and in tissue culture cells, and Hook proteins were found to form homo- and heterodimers. The ∼500-kDa FHF complex contained all three Hook proteins, and small interfering RNA depletion experiments suggest that Hook proteins can interact interchangeably within this complex. Hook proteins as well as FTS interact with members of both the class B and class C components of the homotypic vesicular protein sorting (HOPS) complex. Depletion of FTS by RNA interference affects both the trafficking of epidermal growth factor from early-to-late endosome/lysosomes and the efficiency by which overexpression of the HOPS component Vps18 promotes clustering of lysosomal-associated membrane protein 1-positive endosome/lysosomes. These data suggest that the FTS/Hook/FHIP complex functions to promote vesicle trafficking and/or fusion via the HOPS complex.

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Schroeder, Courtney M., and Ronald D. Vale. "Assembly and activation of dynein–dynactin by the cargo adaptor protein Hook3." Journal of Cell Biology 214, no. 3 (August 1, 2016): 309–18. http://dx.doi.org/10.1083/jcb.201604002.

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Metazoan cytoplasmic dynein moves processively along microtubules with the aid of dynactin and an adaptor protein that joins dynein and dynactin into a stable ternary complex. Here, we examined how Hook3, a cargo adaptor involved in Golgi and endosome transport, forms a motile dynein–dynactin complex. We show that the conserved Hook domain interacts directly with the dynein light intermediate chain 1 (LIC1). By solving the crystal structure of the Hook domain and using structure-based mutagenesis, we identify two conserved surface residues that are each critical for LIC1 binding. Hook proteins with mutations in these residues fail to form a stable dynein–dynactin complex, revealing a crucial role for LIC1 in this interaction. We also identify a region of Hook3 specifically required for an allosteric activation of processive motility. Our work reveals the structural details of Hook3’s interaction with dynein and offers insight into how cargo adaptors form processive dynein–dynactin motor complexes.

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Zhang, Jun, Rongde Qiu, Herbert N. Arst, Miguel A. Peñalva, and Xin Xiang. "HookA is a novel dynein–early endosome linker critical for cargo movement in vivo." Journal of Cell Biology 204, no. 6 (March 17, 2014): 1009–26. http://dx.doi.org/10.1083/jcb.201308009.

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Cytoplasmic dynein transports membranous cargoes along microtubules, but the mechanism of dynein–cargo interaction is unclear. From a genetic screen, we identified a homologue of human Hook proteins, HookA, as a factor required for dynein-mediated early endosome movement in the filamentous fungus Aspergillus nidulans. HookA contains a putative N-terminal microtubule-binding domain followed by coiled-coil domains and a C-terminal cargo-binding domain, an organization reminiscent of cytoplasmic linker proteins. HookA–early endosome interaction occurs independently of dynein–early endosome interaction and requires the C-terminal domain. Importantly, HookA interacts with dynein and dynactin independently of HookA–early endosome interaction but dependent on the N-terminal part of HookA. Both dynein and the p25 subunit of dynactin are required for the interaction between HookA and dynein–dynactin, and loss of HookA significantly weakens dynein–early endosome interaction, causing a virtually complete absence of early endosome movement. Thus, HookA is a novel linker important for dynein–early endosome interaction in vivo.

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Park, Cheon-Gyu, Yongsoo Park, and Byung-Chang Suh. "The HOOK region of voltage-gated Ca2+ channel β subunits senses and transmits PIP2 signals to the gate." Journal of General Physiology 149, no. 2 (January 13, 2017): 261–76. http://dx.doi.org/10.1085/jgp.201611677.

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The β subunit of voltage-gated Ca2+ (CaV) channels plays an important role in regulating gating of the α1 pore-forming subunit and its regulation by phosphatidylinositol 4,5-bisphosphate (PIP2). Subcellular localization of the CaV β subunit is critical for this effect; N-terminal–dependent membrane targeting of the β subunit slows inactivation and decreases PIP2 sensitivity. Here, we provide evidence that the HOOK region of the β subunit plays an important role in the regulation of CaV biophysics. Based on amino acid composition, we broadly divide the HOOK region into three domains: S (polyserine), A (polyacidic), and B (polybasic). We show that a β subunit containing only its A domain in the HOOK region increases inactivation kinetics and channel inhibition by PIP2 depletion, whereas a β subunit with only a B domain decreases these responses. When both the A and B domains are deleted, or when the entire HOOK region is deleted, the responses are elevated. Using a peptide-to-liposome binding assay and confocal microscopy, we find that the B domain of the HOOK region directly interacts with anionic phospholipids via polybasic and two hydrophobic Phe residues. The β2c-short subunit, which lacks an A domain and contains fewer basic amino acids and no Phe residues in the B domain, neither associates with phospholipids nor affects channel gating dynamically. Together, our data suggest that the flexible HOOK region of the β subunit acts as an important regulator of CaV channel gating via dynamic electrostatic and hydrophobic interaction with the plasma membrane.

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Shen, Yuanying, Chongwen Yu, and Jianping Yang. "A study on fiber motion in the drafting zone and hook removal." Textile Research Journal 90, no. 11-12 (November 22, 2019): 1277–90. http://dx.doi.org/10.1177/0040517519889557.

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In this study, the hook removal of four types of hooks during the drafting process has been investigated, and the theory of fiber straightening was further improved by analyzing the relationship between fiber length, fiber straightness, draft ratio, and the fiber accelerated point. Simultaneously, a time domain model was used to simulate the dynamic drafting process based on the straightening analysis, which provided an approach to capture the dynamic motion of different types of fibers and hook removal in the drafting zone. The model is validated by a previous study and experimental work, with the result that the output fiber straightness is both in a good agreement with those calculated by classical theories and experimental data. The straightening effect of the drafting process on four types of hooks under the same drafting conditions is compared. It is shown that the drafting effect on different types of hooked fibers is varied, with the clumped fiber removed preferentially followed by both end hooks or the trailing hook, whereas the leading hook is the most difficult to remove.

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Horváth, Péter, Takayuki Kato, Tomoko Miyata, and Keiichi Namba. "Structure of Salmonella Flagellar Hook Reveals Intermolecular Domain Interactions for the Universal Joint Function." Biomolecules 9, no. 9 (September 9, 2019): 462. http://dx.doi.org/10.3390/biom9090462.

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The bacterial flagellum is a motility organelle consisting of a rotary motor and a long helical filament as a propeller. The flagellar hook is a flexible universal joint that transmits motor torque to the filament in its various orientations that change dynamically between swimming and tumbling of the cell upon switching the motor rotation for chemotaxis. Although the structures of the hook and hook protein FlgE from different bacterial species have been studied, the structure of Salmonella hook, which has been studied most over the years, has not been solved at a high enough resolution to allow building an atomic model of entire FlgE for understanding the mechanisms of self-assembly, stability and the universal joint function. Here we report the structure of Salmonella polyhook at 4.1 Å resolution by electron cryomicroscopy and helical image analysis. The density map clearly revealed folding of the entire FlgE chain forming the three domains D0, D1 and D2 and allowed us to build an atomic model. The model includes domain Dc with a long β-hairpin structure that connects domains D0 and D1 and contributes to the structural stability of the hook while allowing the flexible bending of the hook as a molecular universal joint.

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Cayuela, María L., Montserrat Elías-Arnanz, Marcos Peñalver-Mellado, S. Padmanabhan, and Francisco J. Murillo. "The Stigmatella aurantiaca Homolog of Myxococcus xanthus High-Mobility-Group A-Type Transcription Factor CarD: Insights into the Functional Modules of CarD and Their Distribution in Bacteria." Journal of Bacteriology 185, no. 12 (June 15, 2003): 3527–37. http://dx.doi.org/10.1128/jb.185.12.3527-3537.2003.

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ABSTRACT Transcriptional factor CarD is the only reported prokaryotic analog of eukaryotic high-mobility-group A (HMGA) proteins, in that it has contiguous acidic and AT hook DNA-binding segments and multifunctional roles in Myxococcus xanthus carotenogenesis and fruiting body formation. HMGA proteins are small, randomly structured, nonhistone, nuclear architectural factors that remodel DNA and chromatin structure. Here we report on a second AT hook protein, CarDSa, that is very similar to CarD and that occurs in the bacterium Stigmatella aurantiaca. CarDSa has a C-terminal HMGA-like domain with three AT hooks and a highly acidic adjacent region with one predicted casein kinase II (CKII) phosphorylation site, compared to the four AT hooks and five CKII sites in CarD. Both proteins have a nearly identical 180-residue N-terminal segment that is absent in HMGA proteins. In vitro, CarDSa exhibits the specific minor-groove binding to appropriately spaced AT-rich DNA that is characteristic of CarD or HMGA proteins, and it is also phosphorylated by CKII. In vivo, CarDSa or a variant without the single CKII phosphorylation site can replace CarD in M. xanthus carotenogenesis and fruiting body formation. These two cellular processes absolutely require that the highly conserved N-terminal domain be present. Thus, three AT hooks are sufficient, the N-terminal domain is essential, and phosphorylation in the acidic region by a CKII-type kinase can be dispensed with for CarD function in M. xanthus carotenogenesis and fruiting body development. Whereas a number of hypothetical proteins homologous to the N-terminal region occur in a diverse array of bacterial species, eukaryotic HMGA-type domains appear to be confined primarily to myxobacteria.

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Krämer, H., and M. Phistry. "Mutations in the Drosophila hook gene inhibit endocytosis of the boss transmembrane ligand into multivesicular bodies." Journal of Cell Biology 133, no. 6 (June 15, 1996): 1205–15. http://dx.doi.org/10.1083/jcb.133.6.1205.

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Transmembrane ligands can be internalized across cell boundaries into receptor-expressing cells. In the developing Drosophila eye imaginal disc, the bride of sevenless transmembrane protein (boss) is expressed on the surface of R8 cells. After internalization into neighboring R7 cells, the boss protein accumulates in multivesicular bodies. In a search for genes that affect this cell-type-specific pattern of boss endocytosis, we found that mutations in the hook gene inhibit the accumulation of boss in multivesicular bodies of R7 cells. In addition, hook flies exhibit pleiotropic phenotypes including abnormal bristle morphology and eye degeneration. The wild-type-pattern of boss endocytosis was restored in hook mutants by a genomic rescue fragment containing the hook gene or by a hook cDNA expressed in R7 cells under control of a sevenless (sev) enhancer. The hook gene encodes a novel cytoplasmic protein of 679 amino acids with a central coiled-coil domain of some 200 amino acids. Truncated, epitope-tagged hook proteins coimmunoprecipitated the full-length protein, indicating dimerization mediated by the coiled-coil domain. The hook protein localizes to vesicular structures that are part of the endocytic compartment. The requirement of the hook protein in R7 cells for the accumulation of boss protein in multivesicular bodies, and the localization of the hook protein to endocytic vesicles indicate that the hook gene encodes a novel component of the endocytic compartment that plays an important role in the endocytosis of transmembrane ligands or their transport to multivesicular bodies.

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Ciampi, Raffaele, Thomas J. Giordano, Kathryn Wikenheiser-Brokamp, Ronald J. Koenig, and Yuri E. Nikiforov. "HOOK3-RET: a novel type of RET/PTC rearrangement in papillary thyroid carcinoma." Endocrine-Related Cancer 14, no. 2 (June 2007): 445–52. http://dx.doi.org/10.1677/erc-07-0039.

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Chromosomal rearrangements of the RET proto-oncogene (RET/PTC) are the common feature of papillary thyroid carcinoma (PTC). In this study, we report the identification, cloning, and functional characterization of a novel type of RET/PTC rearrangement that results from the fusion of the 3′-portion of RET coding for the tyrosine kinase (TK) domain of the receptor to the 5′-portion of the Homo sapiens hook homolog 3 (HOOK3) gene. The novel fusion was identified in a case of PTC that revealed a gene expression signature characteristic of RET/PTC on DNA microarray analysis, but was negative for the most common types of RET rearrangement. A fusion product between exon 11 of HOOK3 and exon 12 of RET gene was identified by 5′RACE, and the presence of chimeric HOOK3-RET protein of 88 kDa was detected by western blot analysis with an anti-RET antibody. The protein is predicted to contain a portion of the coiled-coil domains of HOOK3 and the intact TK domain of RET. Expression of the HOOK3-RET cDNA in NIH3T3 cells resulted in the formation of transformed foci and in tumor formation after injection into nude mice, confirming the oncogenic nature of HOOK3-RET.

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Laumer, I. B., T. Bugnyar, S. A. Reber, and A. M. I. Auersperg. "Can hook-bending be let off the hook? Bending/unbending of pliant tools by cockatoos." Proceedings of the Royal Society B: Biological Sciences 284, no. 1862 (September 6, 2017): 20171026. http://dx.doi.org/10.1098/rspb.2017.1026.

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The spontaneous crafting of hook-tools from bendable material to lift a basket out of a vertical tube in corvids has widely been used as one of the prime examples of animal tool innovation. However, it was recently suggested that the animals' solution was hardly innovative but strongly influenced by predispositions from habitual tool use and nest building. We tested Goffin's cockatoo, which is neither a specialized tool user nor a nest builder, on a similar task set-up. Three birds individually learned to bend hook tools from straight wire to retrieve food from vertical tubes and four subjects unbent wire to retrieve food from horizontal tubes. Pre-experience with ready-made hooks had some effect but was not necessary for success. Our results indicate that the ability to represent and manufacture tools according to a current need does not require genetically hardwired behavioural routines, but can indeed arise innovatively from domain general cognitive processing.

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Singh, Gyanendra, Siddhesh Aras, Arnold H. Zea, Shahriar Koochekpour, and Ashok Aiyar. "Optimal Transactivation by Epstein-Barr Nuclear Antigen 1 Requires the UR1 and ATH1 Domains." Journal of Virology 83, no. 9 (February 25, 2009): 4227–35. http://dx.doi.org/10.1128/jvi.02578-08.

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ABSTRACT Epstein-Barr nuclear antigen 1 (EBNA1) is essential for Epstein-Barr virus to immortalize naïve B cells. EBNA1 transactivates viral promoters for genes that are necessary for immortalization when it is bound to a cluster of 20 cognate binding sites, termed the family of repeats. A region of EBNA1 from amino acids (aa) 40 to 89, termed linking region 1 (LR1), has been identified previously as being sufficient for transactivation. LR1 contains two domains that are conserved in the EBNA1 orthologs of other gamma herpesviruses. The first of these, termed unique region 1 (UR1), corresponds to aa 65 to 89 of EBNA1. UR1 is necessary for transactivation and contains a conserved recognition site for cyclic AMP-dependent protein kinase (PKA), corresponding to serine 78 of EBNA1. We have pharmacologically modulated PKA activity to determine if PKA controls EBNA1's ability to transactivate. Our results indicate that PKA activators and inhibitors do not affect transactivation by EBNA1. In addition, site-directed mutagenesis demonstrates that transactivation is not influenced by the phosphorylation status of serine 78 in the UR1 domain. The second conserved domain within LR1 is a glycine-arginine repeat, corresponding to aa 40 to 54 of EBNA1. This domain, termed ATH1, functions as an AT-hook, a DNA-binding motif found in architectural transcription factors such as HMGA1a. We demonstrate that deletion of the ATH1 domain decreases EBNA1 transactivation ability, which is consistent with a transcriptional role for ATH1. Furthermore, transactivation is restored when ATH1 is replaced by equivalent AT-hook motifs from HMGA1a. Our data strongly indicate a role for AT-hooks in EBNA1's ability to transactivate, a function necessary for EBV to immortalize naïve B-cells.

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Walters, Matthew S., Kersten T. Hall, and Adrian Whitehouse. "The Herpesvirus Saimiri Open Reading Frame (ORF) 50 (Rta) Protein Contains an AT Hook Required for Binding to the ORF 50 Response Element in Delayed-Early Promoters." Journal of Virology 78, no. 9 (May 1, 2004): 4936–42. http://dx.doi.org/10.1128/jvi.78.9.4936-4942.2004.

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ABSTRACT The herpesvirus saimiri open reading frame (ORF) 50 encodes two proteins, which activate transcription directly, following interactions with delayed-early (DE) promoters containing a specific motif. In this report, we demonstrate that ORF 50 contains a DNA binding domain that has homology to an AT hook DNA binding motif. Deletion analysis of this domain reduces ORF 50-mediated transactivation of the DE ORF 6 and ORF 57 promoters by 100 and 90%, respectively. Furthermore, gel retardation experiments demonstrated that the AT hook motif is required for binding the ORF 50 response element in the promoters of DE genes. Single site-directed mutagenesis of the AT hook revealed that mutation of the glycine residue at position 408 to an alanine reduces ORF 50 transactivation of the ORF 57 promoter by 40%. Moreover, the mutation of multiple basic residues in conjunction with the glycine residue within the core element of the AT hook abolishes ORF 50-mediated transactivation. In addition, p50GFPΔAT-hook is capable of functioning as a trans-dominant mutant, leading to a reduction in virus production of approximately 50% compared to that for wild-type ORF 50.

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Uedaira, Hatsuho, Hisayuki Morii, Miyuki Ishimura, Hisaaki Taniguchi, Keiichi Namba, and Ferenc Vonderviszt. "Domain organization of flagellar hook protein from Salmonella typhimurium." FEBS Letters 445, no. 1 (February 19, 1999): 126–30. http://dx.doi.org/10.1016/s0014-5793(99)00110-6.

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Hohl, Marcel, Tomasz Kochańczyk, Cristina Tous, Andrés Aguilera, Artur Krężel, and John H. J. Petrini. "Interdependence of the Rad50 Hook and Globular Domain Functions." Molecular Cell 57, no. 3 (February 2015): 479–91. http://dx.doi.org/10.1016/j.molcel.2014.12.018.

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Moriya, Nao, Tohru Minamino, Hedda Ferris, Yusuke V. Morimoto, Masamichi Ashihara, Takayuki Kato, and Keiichi Namba. "Role of the Dc domain of the bacterial hook protein FlgE in hook assembly and function." BIOPHYSICS 9 (2013): 63–72. http://dx.doi.org/10.2142/biophysics.9.63.

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Qiu, Rongde, Jun Zhang, and Xin Xiang. "LIS1 regulates cargo-adapter–mediated activation of dynein by overcoming its autoinhibition in vivo." Journal of Cell Biology 218, no. 11 (September 27, 2019): 3630–46. http://dx.doi.org/10.1083/jcb.201905178.

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Deficiency of the LIS1 protein causes lissencephaly, a brain developmental disorder. Although LIS1 binds the microtubule motor cytoplasmic dynein and has been linked to dynein function in many experimental systems, its mechanism of action remains unclear. Here, we revealed its function in cargo-adapter–mediated dynein activation in the model organism Aspergillus nidulans. Specifically, we found that overexpressed cargo adapter HookA (Hook in A. nidulans) missing its cargo-binding domain (ΔC-HookA) causes dynein and its regulator dynactin to relocate from the microtubule plus ends to the minus ends, and this relocation requires LIS1 and its binding protein, NudE. Astonishingly, the requirement for LIS1 or NudE can be bypassed to a significant extent by mutations that prohibit dynein from forming an autoinhibited conformation in which the motor domains of the dynein dimer are held close together. Our results suggest a novel mechanism of LIS1 action that promotes the switch of dynein from the autoinhibited state to an open state to facilitate dynein activation.

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Chen, Wei-Yu, Cheng-Yang Liu, Yu-Kai Hsieh, Oleg V. Minin, and Igor V. Minin. "Photonic Hook with Modulated Bending Angle Formed by Using Triangular Mesoscale Janus Prisms." Photonics 9, no. 12 (December 8, 2022): 948. http://dx.doi.org/10.3390/photonics9120948.

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In this study, we propose a novel design of triangular mesoscale Janus prisms for the generation of the long photonic hook. Numerical simulations based on the finite-difference time-domain method are used to examine the formation mechanism of the photonic hook. The electric intensity distributions near the micro-prisms are calculated for operation at different refractive indices and spaces of the two triangular micro-prisms. The asymmetric vortices of intensity distributions result in a long photonic hook with a large bending angle. The length and the bending angle of the photonic hook are efficiently modulated by changing the space between the two triangular micro-prisms. Moreover, the narrow width of the photonic hook is achieved beyond the diffraction limit. The triangular Janus micro-prisms have high potential for practical applications in optical tweezers, nanoparticle sorting and manipulation and photonic circuits.

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Muller, Yves A., Sigrun Häge, Sewar Alkhashrom, Tobias Höllriegl, Sebastian Weigert, Simon Dolles, Kerstin Hof, et al. "High-resolution crystal structures of two prototypical β- and γ-herpesviral nuclear egress complexes unravel the determinants of subfamily specificity." Journal of Biological Chemistry 295, no. 10 (January 24, 2020): 3189–201. http://dx.doi.org/10.1074/jbc.ra119.011546.

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Herpesviruses uniquely express two essential nuclear egress-regulating proteins forming a heterodimeric basic structure of the nuclear egress complex (core NEC). These core NECs serve as a hexameric lattice-structured platform for capsid docking and recruit viral and cellular NEC-associated factors that jointly exert nuclear lamina- and membrane-rearranging functions (multicomponent NEC). Here, we report the X-ray structures of β- and γ-herpesvirus core NECs obtained through an innovative recombinant expression strategy based on NEC-hook::NEC-groove protein fusion constructs. This approach yielded the first structure of γ-herpesviral core NEC, namely the 1.56 Å structure of Epstein-Barr virus (EBV) BFRF1–BFLF2, as well as an increased resolution 1.48 Å structure of human cytomegalovirus (HCMV) pUL50-pUL53. Detailed analysis of these structures revealed that the prominent hook segment is absolutely required for core NEC formation and contributes approximately 80% of the interaction surface of the globular domains of NEC proteins. Moreover, using HCMV::EBV hook domain swap constructs, computational prediction of the roles of individual hook residues for binding, and quantitative binding assays with synthetic peptides presenting the HCMV- and EBV-specific NEC hook sequences, we characterized the unique hook-into-groove NEC interaction at various levels. Although the overall physicochemical characteristics of the protein interfaces differ considerably in these β- and γ-herpesvirus NECs, the binding free energy contributions of residues displayed from identical positions are similar. In summary, the results of our study reveal critical details of the molecular mechanism of herpesviral NEC interactions and highlight their potential as an antiviral drug target.

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Roset, R., A. Inagaki, M. Hohl, F. Brenet, J. Lafrance-Vanasse, J. Lange, J. M. Scandura, J. A. Tainer, S. Keeney, and J. H. J. Petrini. "The Rad50 hook domain regulates DNA damage signaling and tumorigenesis." Genes & Development 28, no. 5 (February 14, 2014): 451–62. http://dx.doi.org/10.1101/gad.236745.113.

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Eggenhofer, Elke, Reinhard Rachel, Martin Haslbeck, and Birgit Scharf. "MotD of Sinorhizobium meliloti and Related α-Proteobacteria Is the Flagellar-Hook-Length Regulator and Therefore Reassigned as FliK." Journal of Bacteriology 188, no. 6 (March 15, 2006): 2144–53. http://dx.doi.org/10.1128/jb.188.6.2144-2153.2006.

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ABSTRACT The flagella of the soil bacterium Sinorhizobium meliloti differ from the enterobacterial paradigm in the complex filament structure and modulation of the flagellar rotary speed. The mode of motility control in S. meliloti has a molecular corollary in two novel periplasmic motility proteins, MotC and MotE, that are present in addition to the ubiquitous MotA/MotB energizing proton channel. A fifth motility gene is located in the mot operon downstream of the motB and motC genes. Its gene product was originally designated MotD, a cytoplasmic motility protein having an unknown function. We report here reassignment of MotD as FliK, the regulator of flagellar hook length. The FliK gene is one of the few flagellar genes not annotated in the contiguous flagellar regulon of S. meliloti. Characteristic for its class, the 475-residue FliK protein contains a conserved, compactly folded Flg hook domain in its carboxy-terminal region. Deletion of fliK leads to formation of prolonged flagellar hooks (polyhooks) with missing filament structures. Extragenic suppressor mutations all mapped in the cytoplasmic region of the transmembrane export protein FlhB and restored assembly of a flagellar filament, and thus motility, in the presence of polyhooks. The structural properties of FliK are consistent with its function as a substrate specificity switch of the flagellar export apparatus for switching from rod/hook-type substrates to filament-type substrates.

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Oliver, Antony W., Sarah A. Jones, Stephen Mark Roe, Steve Matthews, Graham H. Goodwin, and Laurence H. Pearl. "Crystal structure of the proximal BAH domain of the polybromo protein." Biochemical Journal 389, no. 3 (July 26, 2005): 657–64. http://dx.doi.org/10.1042/bj20050310.

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The BAH domain (bromo-associated homology domain) was first identified from a repeated motif found in the nuclear protein polybromo – a large (187 kDa) modular protein comprising six bromodomains, two BAH domains and an HMG box. To date, the BAH domain has no ascribed function, although it is found in a wide range of proteins that contain additional domains involved in either transcriptional regulation (e.g. SET, PHD and bromodomain) and/or DNA binding (HMG box and AT hook). The molecular function of polybromo itself also remains unclear, but it has been identified as a key component of an SWI/SNF (switching/sucrose non-fermenting)-related, ATP-dependent chromatin-remodelling complex PBAF (polybromo, BRG1-associated factors; also known as SWI/SNF-B or SWI/SNFβ). We present in this paper the crystal structure of the proximal BAH domain from chicken polybromo (BAH1), at a resolution of 1.6 Å (1 Å=0.1 nm). Structure-based sequence analysis reveals several features that may be involved in mediating protein–protein interactions.

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Moriya, N., T. Minamino, May Kihara, Robert Macnab, and K. Namba. "1P187 The role of the C-terminal domain of Salmonella hook-capping protein FlgD in flagellar hook assembly." Seibutsu Butsuri 45, supplement (2005): S78. http://dx.doi.org/10.2142/biophys.45.s78_3.

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Uchida, Kaoru, Kohei Dono, and Shin-Ichi Aizawa. "Identification of the Key Sequence in the FliK C-Terminal Domain for Substrate Specificity Switching in the Flagellar Protein Secretion." Journal of Bacteriology 198, no. 3 (November 2, 2015): 410–15. http://dx.doi.org/10.1128/jb.00712-15.

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ABSTRACTThe flagellar hook is a short tubular structure located between the external filament and the membrane-bound basal body. The average hook length is 55 nm and is determined by the soluble protein FliK and the integral membrane protein FlhB. Hook elongation is terminated by FliK-mediated cessation of hook protein secretion, followed by the secretion of filamentous proteins. This process is referred to as the substrate specificity switch. Switching of the secretion modes results from a direct interaction between the FliK C-terminal domain (FliKC) and the secretion gate in FlhB. FliKCconsists of two α-helices and four β-strands. Loop 2 connects the first two β-sheets and contains a conserved sequence of 9 residues. Genetic and physiological analyses of variousfliKpartial deletion mutants pointed to loop 2 as essential for induction of a conformational change in the FlhB gate. We constructed single-amino-acid substitutions in the conserved region of loop 2 of FliK and discovered that the loop sequence LRL is essential for the timely switching of secretion modes.IMPORTANCEFlagellar protein secretion is controlled by the soluble protein FliK. We discovered that the loop 2 sequence LRL in the FliK C terminus was essential for timely switching of secretion modes. This mechanism is applicable to type three secretions systems that secrete virulence factors in bacterial pathogens.

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Samatey, F. A., H. Matsunami, K. Imada, S. Nagashima, T. R. Shaikh, D. Thomas, D. J. DeRosier, and K. Namba. "Twist and curvature formation of the hook: a two-domain movement." Acta Crystallographica Section A Foundations of Crystallography 60, a1 (August 26, 2004): s157. http://dx.doi.org/10.1107/s0108767304096904.

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Morgan, David Gene, Robert M. Macnab, Noreen R. Francis, and David J. DeRosier. "Domain Organization of the Subunit of the Salmonella typhimurium Flagellar Hook." Journal of Molecular Biology 229, no. 1 (January 1993): 79–84. http://dx.doi.org/10.1006/jmbi.1993.1009.

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Boex-Fontvieille, Edouard, Sachin Rustgi, Diter von Wettstein, Steffen Reinbothe, and Christiane Reinbothe. "Water-soluble chlorophyll protein is involved in herbivore resistance activation during greening of Arabidopsis thaliana." Proceedings of the National Academy of Sciences 112, no. 23 (May 27, 2015): 7303–8. http://dx.doi.org/10.1073/pnas.1507714112.

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Water-soluble chlorophyll proteins (WSCPs) constitute a small family of unusual chlorophyll (Chl)-binding proteins that possess a Kunitz-type protease inhibitor domain. In Arabidopsis thaliana, a WSCP has been identified, named AtWSCP, that forms complexes with Chl and the Chl precursor chlorophyllide (Chlide) in vitro. AtWSCP exhibits a quite unexpected expression pattern for a Chl binding protein and accumulated to high levels in the apical hook of etiolated plants. AtWSCP expression was negatively light-regulated. Transgenic expression of AtWSCP fused to green fluorescent protein (GFP) revealed that AtWSCP is localized to cell walls/apoplastic spaces. Biochemical assays identified AtWSCP as interacting with RD21 (RESPONSIVE TO DESICCATION 21), a granulin domain-containing cysteine protease implicated in stress responses and defense. Reconstitution experiments showed tight interactions between RD21 and WSCP that were relieved upon Chlide binding. Laboratory feeding experiments with two herbivorous isopod crustaceans, Porcellio scaber (woodlouse) and Armadillidium vulgare (pillbug), identified the apical hook as Achilles’ heel of etiolated plants and that this was protected by RD21 during greening. Because Chlide is formed in the apical hook during seedling emergence from the soil, our data suggest an unprecedented mechanism of herbivore resistance activation that is triggered by light and involves AtWSCP.

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Minamino, Tohru, and Robert M. Macnab. "Domain Structure of Salmonella FlhB, a Flagellar Export Component Responsible for Substrate Specificity Switching." Journal of Bacteriology 182, no. 17 (September 1, 2000): 4906–14. http://dx.doi.org/10.1128/jb.182.17.4906-4914.2000.

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ABSTRACT We have investigated the properties of the cytoplasmic domain (FlhBC) of the 383-amino-acid Salmonellamembrane protein FlhB, a component of the type III flagellar export apparatus. FlhB, along with the hook-length control protein FliK, mediates the switching of export specificity from rod- and hook-type substrates to filament-type substrates during flagellar morphogenesis. Wild-type FlhBC was unstable (half-life, ca. 5 min), being specifically cleaved at Pro-270 into two polypeptides, FlhBCN and FlhBCC, which retained the ability to interact with each other after cleavage. Full-length wild-type FlhB was also subject to cleavage. Coproduction of the cleavage products, FlhBΔCC (i.e., the N-terminal transmembrane domain FlhBTM plus FlhBCN) and FlhBCC, resulted in restoration of both motility and flagellar protein export to an flhB mutant host, indicating that the two polypeptides were capable of productive association. Mutant FlhB proteins that can undergo switching of substrate specificity even in the absence of FliK were much more resistant to cleavage (half-lives, 20 to 60 min). The cleavage products of wild-type FlhBC, existing as a FlhBCN–FlhBCC complex on an affinity blot membrane, bound the rod- and hook-type substrate FlgD more strongly than the filament-type substrate FliC. In contrast, the intact form of FlhBC (mutant or wild type) or the FlhBCC polypeptide alone bound FlgD and FliC to about the same extent. FlhBCN by itself did not bind substrates appreciably. We propose that FlhBC has two substrate specificity states and that a conformational change, mediated by the interaction between FlhBCN and FlhBCC, is responsible for the specificity switching process. FliK itself is an export substrate; its binding properties for FlhBC resemble those of FlgD and do not provide any evidence for a physical interaction beyond that of the export process.

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Xu, Yifeng, Eng-Seng Gan, and Toshiro Ito. "The AT-hook/PPC domain protein TEK negatively regulates floral repressors includingMAF4andMAF5." Plant Signaling & Behavior 8, no. 8 (August 2013): e25006. http://dx.doi.org/10.4161/psb.25006.

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Wiltzius, Jed J. W., Marcel Hohl, James C. Fleming, and John H. J. Petrini. "The Rad50 hook domain is a critical determinant of Mre11 complex functions." Nature Structural & Molecular Biology 12, no. 5 (April 24, 2005): 403–7. http://dx.doi.org/10.1038/nsmb928.

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Cahill, D., and J. P. Carney. "Dimerization of the Rad50 protein is independent of the conserved hook domain." Mutagenesis 22, no. 4 (April 9, 2007): 269–74. http://dx.doi.org/10.1093/mutage/gem011.

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Darvekar, Sagar, Sylvia Sagen Johnsen, Agnete Bratsberg Eriksen, Terje Johansen, and Eva Sjøttem. "Identification of two independent nucleosome-binding domains in the transcriptional co-activator SPBP." Biochemical Journal 442, no. 1 (January 27, 2012): 65–75. http://dx.doi.org/10.1042/bj20111230.

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Transcriptional regulation requires co-ordinated action of transcription factors, co-activator complexes and general transcription factors to access specific loci in the dense chromatin structure. In the present study we demonstrate that the transcriptional co-regulator SPBP [stromelysin-1 PDGF (platelet-derived growth factor)-responsive element binding protein] contains two independent chromatin-binding domains, the SPBP-(1551–1666) region and the C-terminal extended PHD [ePHD/ADD (extended plant homeodomain/ATRX-DNMT3-DNMT3L)] domain. The region 1551–1666 is a novel core nucleosome-interaction domain located adjacent to the AT-hook motif in the DNA-binding domain. This novel nucleosome-binding region is critically important for proper localization of SPBP in the cell nucleus. The ePHD/ADD domain associates with nucleosomes in a histone tail-dependent manner, and has significant impact on the dynamic interaction between SPBP and chromatin. Furthermore, SPBP and its homologue RAI1 (retinoic-acid-inducible protein 1), are strongly enriched on chromatin in interphase HeLa cells, and both proteins display low nuclear mobility. RAI1 contains a region with homology to the novel nucleosome-binding region SPBP-(1551–1666) and an ePHD/ADD domain with ability to bind nucleosomes. These results indicate that the transcriptional co-regulator SPBP and its homologue RAI1 implicated in Smith–Magenis syndrome and Potocki–Lupski syndrome both belong to the expanding family of chromatin-binding proteins containing several domains involved in specific chromatin interactions.

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Ko, Josephine Mun Yee, Shiu Yeung Lam, Lvwen Ning, Annie Wai Yeeng Chai, Lisa Chan Lei, Sheyne Sta Ana Choi, Carissa Wing Yan Wong, and Maria Li Lung. "RAD50 Loss of Function Variants in the Zinc Hook Domain Associated with Higher Risk of Familial Esophageal Squamous Cell Carcinoma." Cancers 13, no. 18 (September 21, 2021): 4715. http://dx.doi.org/10.3390/cancers13184715.

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Unbiased whole-exome sequencing approaches in familial esophageal squamous cell carcinoma (ESCC) initially prioritized RAD50 as a candidate cancer predisposition gene. The combined study with 3289 Henan individuals from Northern China identified two pathogenic RAD50 protein truncation variants, p.Q672X and a recurrent p.K722fs variant at the zinc hook domain significantly conferring increased familial ESCC risk. Effects of ~10-fold higher familial ESCC risk were observed, when compared to East Asians from the gnomAD database. Functional characterization suggested that the RAD50Q672X mutation contributes a dominant-negative effect in DNA repair of double-stranded breaks. Overexpression of the RAD50Q672X and RAD50L1264F missense mutation also sensitized cell death upon replication stress stimuli induced by formaldehyde treatment and the CHK1 inhibitor, AZD7762. Our study suggested the novel insight of the potential for synthetic lethal therapeutic options for RAD50Q672X and the East-Asian-specific RAD50L1264F variants and CHK1 inhibitors. Our study also suggested the association of RAD50 LOF variants in the zinc hook domain with a higher risk of familial ESCC in Chinese.

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Garvey, Daniel. "The Back Page: My Favorite Lesson: Chess Piece(wise) Project." Mathematics Teacher 104, no. 5 (December 2010): 400. http://dx.doi.org/10.5951/mt.104.5.0400.

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One of my favorite lessons is a project I call Chess Piece(wise). I give this project to my precalculus students after we have discussed domain and range and piecewise-defined functions. Referring to the game of chess and using manipulatives (chessboards and chess pieces) tend to “hook” students. The project challenges them to define piecewise models symbolically, numerically, and graphically and to determine the domain and range of those models. Moreover, students model something that is real and not typically modeled in a mathematics course.

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Garvey, Daniel. "The Back Page: My Favorite Lesson: Chess Piece(wise) Project." Mathematics Teacher 104, no. 5 (December 2010): 400. http://dx.doi.org/10.5951/mt.104.5.0400.

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One of my favorite lessons is a project I call Chess Piece(wise). I give this project to my precalculus students after we have discussed domain and range and piecewise-defined functions. Referring to the game of chess and using manipulatives (chessboards and chess pieces) tend to “hook” students. The project challenges them to define piecewise models symbolically, numerically, and graphically and to determine the domain and range of those models. Moreover, students model something that is real and not typically modeled in a mathematics course.

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Samatey, Fadel, H. Matsunami, K. Imada, S. Nagashima, and K. Namba. "Structural basis of twist and curvature formation of the hook : two-domain movement." Seibutsu Butsuri 43, supplement (2003): S43. http://dx.doi.org/10.2142/biophys.43.s43_4.

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Takahashi, N., S. Shibata, S. Aizawa, and Huehes Kelly. "1P186 Roles of FliK central domain in the hook-length control in Salmonella." Seibutsu Butsuri 45, supplement (2005): S78. http://dx.doi.org/10.2142/biophys.45.s78_2.

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Minamino, Tohru, Yumiko Saijo-Hamano, Yukio Furukawa, Bertha González-Pedrajo, Robert M. Macnab, and Keiichi Namba. "Domain Organization and Function of Salmonella FliK, a Flagellar Hook-length Control Protein." Journal of Molecular Biology 341, no. 2 (August 2004): 491–502. http://dx.doi.org/10.1016/j.jmb.2004.06.012.

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Li, Huimin, Ruixue Hu, Simin Xu, Zeqi Dai, Xue Wu, Jing Hu, and Xing Liao. "Tripterygium wilfordii Hook. f. Preparations for Rheumatoid Arthritis: An Overview of Systematic Reviews." Evidence-Based Complementary and Alternative Medicine 2022 (April 12, 2022): 1–18. http://dx.doi.org/10.1155/2022/3151936.

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Objectives. To summarize the quantity and quality of evidence for using Tripterygium wilfordii Hook. f. (TwHF) preparations in patients with rheumatoid arthritis (RA) and to find the reasons of the disparity by comprehensively appraising the related systematic reviews (SRs). Methods. We performed an overview of evidence for the effectiveness and safety of TwHF preparations for patients with RA. We searched seven literature databases from inception to July 15, 2021. We included SRs of TwHF preparations in the treatment of RA. Four tools were used to evaluate the reporting quality, methodological quality, risk of bias, and the certainty of evidence for the included SRs, which are the PRISMA, the AMSTAR-2, the ROBIS, and the GRADE approach. Results. We included 27 SRs (with 385 studies and 33,888 participants) for this overview. The AMSTAR-2 showed that 19 SRs had critically low methodological quality and the remaining 8 had low methodological quality. The rate of overlaps was 68.31% (263/385), and the CCA (corrected covered area) was 0.53, which indicated the degree of overlap is slight. Based on the assessment of ROBIS, all 27 SRs were rated as low risk in phase 1; one SR was rated as low risk in domain 1, 9 SRs were in low risk in domain 2, 16 SRs were in low risk in domain 3, and 16 SRs were in low risk in domain 4 in phase 2; 7 SRs were rated as low risk in phase 3. Among 27 items of PRISMA, 15 items were reported over 70% of compliance, the reporting quality of 16 SRs was rated as “fair,” and 11 were “good.” Using GRADE assessment, moderate quality of evidence was found in 5 outcomes, and 5 outcomes were low quality. Conclusion. The use of TwHF preparations for the treatment of RA may be clinically effective according to the moderate-quality evidence. There are methodological issues, risk of bias, and reporting deficiencies still needed to be improved. SRs with good quality and further randomized clinical trials that focus on clinical important outcomes are needed.

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Honda, Shinji, Vincent T. Bicocca, Jordan D. Gessaman, Michael R. Rountree, Ayumi Yokoyama, Eun Y. Yu, Jeanne M. L. Selker, and Eric U. Selker. "Dual chromatin recognition by the histone deacetylase complex HCHC is required for proper DNA methylation in Neurospora crassa." Proceedings of the National Academy of Sciences 113, no. 41 (September 28, 2016): E6135—E6144. http://dx.doi.org/10.1073/pnas.1614279113.

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DNA methylation, heterochromatin protein 1 (HP1), histone H3 lysine 9 (H3K9) methylation, histone deacetylation, and highly repeated sequences are prototypical heterochromatic features, but their interrelationships are not fully understood. Prior work showed that H3K9 methylation directs DNA methylation and histone deacetylation via HP1 in Neurospora crassa and that the histone deacetylase complex HCHC is required for proper DNA methylation. The complex consists of the chromodomain proteins HP1 and chromodomain protein 2 (CDP-2), the histone deacetylase HDA-1, and the AT-hook motif protein CDP-2/HDA-1–associated protein (CHAP). We show that the complex is required for proper chromosome segregation, dissect its function, and characterize interactions among its components. Our analyses revealed the existence of an HP1-based DNA methylation pathway independent of its chromodomain. The pathway partially depends on CHAP but not on the CDP-2 chromodomain. CDP-2 serves as a bridge between the recognition of H3K9 trimethylation (H3K9me3) by HP1 and the histone deacetylase activity of HDA-1. CHAP is also critical for HDA-1 localization to heterochromatin. Specifically, the CHAP zinc finger interacts directly with the HDA-1 argonaute-binding protein 2 (Arb2) domain, and the CHAP AT-hook motifs recognize heterochromatic regions by binding to AT-rich DNA. Our data shed light on the interrelationships among the prototypical heterochromatic features and support a model in which dual recognition by the HP1 chromodomain and the CHAP AT-hooks are required for proper heterochromatin formation.

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Biringanine, Gabriel, Moustapha Ouedraogo, Bernard Vray, Anne Berit Samuelsen, and Pierre Duez. "Partial Chemical Characterization of Immunomodulatory Polysaccharides from Plantago palmata Hook. f. s. Leaves." International Journal of Carbohydrate Chemistry 2012 (August 9, 2012): 1–7. http://dx.doi.org/10.1155/2012/458456.

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A previous work on Plantago palmata polysaccharides (PS) attributed immunomodulatory properties of leaves to a polysaccharide fraction (PS50) that stimulated NO and TNF-α production by interferon gamma- (IFN-γ-) activated macrophages. The present work aims to elucidate the chemical structure of these immunomodulatory polysaccharides. Size exclusion chromatography showed that the active polymers present an active fraction with a very high molecular weight (about 1200 kDa). These polysaccharides are pectic in nature, with a predominantly unbranched galacturonan domain and with a domain bearing side chains that consist of highly branched arabinan, galactan, and/or arabinogalactan. Comparatively to the well-known Plantago major biologically active PS, Plantago palmata PS50 contained less arabinogalactan-proteins (AGPs) and had a different composition in glucose, galactose, and galacturonic acid. DNA contamination of the polysaccharide was estimated at about 0.04%, a concentration much lower than those reported immunomodulatory in hyaluronic acid preparations (3 to 15%). Therefore, the eventuality of a contaminating DNA-mediated biological activity could be ruled out.

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Machaj, Gabriela, and Dariusz Grzebelus. "Characteristics of the AT-Hook Motif Containing Nuclear Localized (AHL) Genes in Carrot Provides Insight into Their Role in Plant Growth and Storage Root Development." Genes 12, no. 5 (May 18, 2021): 764. http://dx.doi.org/10.3390/genes12050764.

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The AT-hook motif containing nuclear localized (AHL) gene family, controlling various developmental processes, is conserved in land plants. They comprise Plant and Prokaryote Conserved (PPC) domain and one or two AT-hook motifs. DcAHLc1 has been proposed as a candidate gene governing the formation of the carrot storage root. We identified and in-silico characterized carrot AHL proteins, performed phylogenetic analyses, investigated their expression profiles and constructed gene coexpression networks. We found 47 AHL genes in carrot and grouped them into two clades, A and B, comprising 29 and 18 genes, respectively. Within Clade-A, we distinguished three subclades, one of them grouping noncanonical AHLs differing in their structure (two PPC domains) and/or cellular localization (not nucleus). Coexpression network analysis attributed AHLs expressed in carrot roots into four of the 72 clusters, some of them showing a large number of interactions. Determination of expression profiles of AHL genes in various tissues and samples provided basis to hypothesize on their possible roles in the development of the carrot storage root. We identified a group of rapidly evolving noncanonical AHLs, possibly differing functionally from typical AHLs, as suggested by their expression profiles and their predicted cellular localization. We pointed at several AHLs likely involved in the development of the carrot storage root.

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Ng, Kian-Hong, and Toshiro Ito. "Shedding light on the role of AT-hook/PPC domain protein in Arabidopsis thaliana." Plant Signaling & Behavior 5, no. 2 (February 2010): 200–201. http://dx.doi.org/10.4161/psb.5.2.11111.

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Brunet, Sylvain, Michelle A. Emrick, Martin Sadilek, Todd Scheuer, and William A. Catterall. "Phosphorylation sites in the Hook domain of CaVβ subunits differentially modulate CaV1.2 channel function." Journal of Molecular and Cellular Cardiology 87 (October 2015): 248–56. http://dx.doi.org/10.1016/j.yjmcc.2015.08.006.

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Ma, Yue, Emily L. Niemitz, Patricia A. Nambu, Xiaoliang Shan, Charles Sackerson, Miki Fujioka, Tadaatsu Goto, and John R. Nambu. "Gene regulatory functions of Drosophila Fish-hook, a high mobility group domain Sox protein." Mechanisms of Development 73, no. 2 (May 1998): 169–82. http://dx.doi.org/10.1016/s0925-4773(98)00050-1.

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Xu, Miaojing, Pingping Song, Wei Huang, Rongni He, Yong He, Xiao Zhou, Yong Gu, Suyue Pan, and Yafang Hu. "Disruption of AT-hook 1 domain in MeCP2 protein caused behavioral abnormality in mice." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1864, no. 2 (February 2018): 347–58. http://dx.doi.org/10.1016/j.bbadis.2017.10.022.

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Prescott, Jason D., Karen S. N. Koto, Meenakshi Singh, and Arthur Gutierrez-Hartmann. "The ETS Transcription Factor ESE-1 Transforms MCF-12A Human Mammary Epithelial Cells via a Novel Cytoplasmic Mechanism." Molecular and Cellular Biology 24, no. 12 (June 15, 2004): 5548–64. http://dx.doi.org/10.1128/mcb.24.12.5548-5564.2004.

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ABSTRACT Several different transcription factors, including estrogen receptor, progesterone receptor, and ETS family members, have been implicated in human breast cancer, indicating that transcription factor-induced alterations in gene expression underlie mammary cell transformation. ESE-1 is an epithelium-specific ETS transcription factor that contains two distinguishing domains, a serine- and aspartic acid-rich (SAR) domain and an AT hook domain. ESE-1 is abundantly expressed in human breast cancer and trans-activates epithelium-specific gene promoters in transient transfection assays. While it has been presumed that ETS factors transform mammary epithelial cells via their nuclear transcriptional functions, here we show (i) that ESE-1 protein is cytoplasmic in human breast cancer cells; (ii) that stably expressed green fluorescent protein-ESE-1 transforms MCF-12A human mammary epithelial cells; and (iii) that the ESE-1 SAR domain, acting in the cytoplasm, is necessary and sufficient to mediate this transformation. Deletion of transcriptional regulatory or nuclear localization domains does not impair ESE-1-mediated transformation, whereas fusing the simian virus 40 T-antigen nuclear localization signal to various ESE-1 constructs, including the SAR domain alone, inhibits their transforming capacity. Finally, we show that the nuclear localization of ESE-1 protein induces apoptosis in nontransformed mammary epithelial cells via a transcription-dependent mechanism. Together, our studies reveal two distinct ESE-1 functions, apoptosis and transformation, where the ESE-1 transcription activation domain contributes to apoptosis and the SAR domain mediates transformation via a novel nonnuclear, nontranscriptional mechanism. These studies not only describe a unique ETS factor transformation mechanism but also establish a new paradigm for cell transformation in general.

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Broster Reix, Christine E., Célia Florimond, Anne Cayrel, Amélie Mailhé, Corentin Agnero-Rigot, Nicolas Landrein, Denis Dacheux, et al. "Bhalin, an Essential Cytoskeleton-Associated Protein of Trypanosoma brucei Linking TbBILBO1 of the Flagellar Pocket Collar with the Hook Complex." Microorganisms 9, no. 11 (November 11, 2021): 2334. http://dx.doi.org/10.3390/microorganisms9112334.

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Background: In most trypanosomes, endo and exocytosis only occur at a unique organelle called the flagellar pocket (FP) and the flagellum exits the cell via the FP. Investigations of essential cytoskeleton-associated structures located at this site have revealed a number of essential proteins. The protein TbBILBO1 is located at the neck of the FP in a structure called the flagellar pocket collar (FPC) and is essential for biogenesis of the FPC and parasite survival. TbMORN1 is a protein that is present on a closely linked structure called the hook complex (HC) and is located anterior to and overlapping the collar. TbMORN1 is essential in the bloodstream form of T. brucei. We now describe the location and function of BHALIN, an essential, new FPC-HC protein. Methodology/Principal Findings: Here, we show that a newly characterised protein, BHALIN (BILBO1 Hook Associated LINker protein), is localised to both the FPC and HC and has a TbBILBO1 binding domain, which was confirmed in vitro. Knockdown of BHALIN by RNAi in the bloodstream form parasites led to cell death, indicating an essential role in cell viability. Conclusions/Significance: Our results demonstrate the essential role of a newly characterised hook complex protein, BHALIN, that influences flagellar pocket organisation and function in bloodstream form T. brucei parasites.

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Richards, Mark W., Jerome Leroy, Wendy S. Pratt, and Annette C. Dolphin. "The HOOK-Domain Between the SH3- and the GK-Domains of CaVβ Subunits Contains Key Determinants Controlling Calcium Channel Inactivation." Channels 1, no. 2 (March 2, 2007): 92–101. http://dx.doi.org/10.4161/chan.4145.

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Garcia, Joshua D., Evan B. Dewey, and Christopher A. Johnston. "Dishevelled Binds the Discs Large ‘Hook’ Domain to Activate GukHolder-Dependent Spindle Positioning in Drosophila." PLoS ONE 9, no. 12 (December 2, 2014): e114235. http://dx.doi.org/10.1371/journal.pone.0114235.

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Cheng, Qing-Ming, and Hong-Cang Yang. "Universal inequalities for eigenvalues of a system of elliptic equations." Proceedings of the Royal Society of Edinburgh: Section A Mathematics 139, no. 2 (March 25, 2009): 273–85. http://dx.doi.org/10.1017/s0308210507000649.

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Let D be a bounded domain in an n-dimensional Euclidean space ℝn. Assume thatare eigenvalues of an eigenvalue problem of a system of n elliptic equations:In particular, when n=3, the eigenvalue problem describes the behaviour of the elastic vibration. We obtain universal inequalities for eigenvalues of the above eigenvalue problem by making use of a direct and explicit method; our results are sharper than one of Hook. Furthermore, a universal inequality for lower-order eigenvalues of the above eigenvalue problem is also derived.

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Journal articles on the topic 'Hook domain'

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