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| | <StructureSection load='6b9h' size='340' side='right'caption='[[6b9h]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='6b9h' size='340' side='right'caption='[[6b9h]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6b9h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B9H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B9H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6b9h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B9H FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HOOK3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6b9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b9h OCA], [http://pdbe.org/6b9h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b9h RCSB], [http://www.ebi.ac.uk/pdbsum/6b9h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b9h ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6b9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b9h OCA], [https://pdbe.org/6b9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b9h RCSB], [https://www.ebi.ac.uk/pdbsum/6b9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b9h ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HOOK3_HUMAN HOOK3_HUMAN]] Probably serves as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking (By similarity). Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex.<ref>PMID:11238449</ref> <ref>PMID:17237231</ref> <ref>PMID:18799622</ref> [[http://www.uniprot.org/uniprot/DC1L1_HUMAN DC1L1_HUMAN]] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress through the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores.<ref>PMID:19229290</ref> | + | [https://www.uniprot.org/uniprot/HOOK3_HUMAN HOOK3_HUMAN] Probably serves as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking (By similarity). Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex.<ref>PMID:11238449</ref> <ref>PMID:17237231</ref> <ref>PMID:18799622</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dominguez, R]] | + | [[Category: Dominguez R]] |
| - | [[Category: Lee, I G]] | + | [[Category: Lee IG]] |
| - | [[Category: Dynactin]]
| + | |
| - | [[Category: Dynein]]
| + | |
| - | [[Category: Effector]]
| + | |
| - | [[Category: Hook]]
| + | |
| - | [[Category: Protein transport-motor protein complex]]
| + | |
| Structural highlights
Function
HOOK3_HUMAN Probably serves as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking (By similarity). Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex.[1] [2] [3]
Publication Abstract from PubMed
Cytoplasmic dynein is the major minus-end-directed microtubule-based motor in cells. Dynein processivity and cargo selectivity depend on cargo-specific effectors that, while generally unrelated, share the ability to interact with dynein and dynactin to form processive dynein-dynactin-effector complexes. How this is achieved is poorly understood. Here, we identify a conserved region of the dynein Light Intermediate Chain 1 (LIC1) that mediates interactions with unrelated dynein-dynactin effectors. Quantitative binding studies map these interactions to a conserved helix within LIC1 and to N-terminal fragments of Hook1, Hook3, BICD2, and Spindly. A structure of the LIC1 helix bound to the N-terminal Hook domain reveals a conformational change that creates a hydrophobic cleft for binding of the LIC1 helix. The LIC1 helix competitively inhibits processive dynein-dynactin-effector motility in vitro, whereas structure-inspired mutations in this helix impair lysosomal positioning in cells. The results reveal a conserved mechanism of effector interaction with dynein-dynactin necessary for processive motility.
A conserved interaction of the dynein light intermediate chain with dynein-dynactin effectors necessary for processivity.,Lee IG, Olenick MA, Boczkowska M, Franzini-Armstrong C, Holzbaur ELF, Dominguez R Nat Commun. 2018 Mar 7;9(1):986. doi: 10.1038/s41467-018-03412-8. PMID:29515126[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Walenta JH, Didier AJ, Liu X, Kramer H. The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins. J Cell Biol. 2001 Mar 5;152(5):923-34. PMID:11238449
- ↑ Sano H, Ishino M, Kramer H, Shimizu T, Mitsuzawa H, Nishitani C, Kuroki Y. The microtubule-binding protein Hook3 interacts with a cytoplasmic domain of scavenger receptor A. J Biol Chem. 2007 Mar 16;282(11):7973-81. Epub 2007 Jan 19. PMID:17237231 doi:http://dx.doi.org/10.1074/jbc.M611537200
- ↑ Xu L, Sowa ME, Chen J, Li X, Gygi SP, Harper JW. An FTS/Hook/p107(FHIP) complex interacts with and promotes endosomal clustering by the homotypic vacuolar protein sorting complex. Mol Biol Cell. 2008 Dec;19(12):5059-71. Epub 2008 Sep 17. PMID:18799622 doi:http://dx.doi.org/E08-05-0473
- ↑ Lee IG, Olenick MA, Boczkowska M, Franzini-Armstrong C, Holzbaur ELF, Dominguez R. A conserved interaction of the dynein light intermediate chain with dynein-dynactin effectors necessary for processivity. Nat Commun. 2018 Mar 7;9(1):986. doi: 10.1038/s41467-018-03412-8. PMID:29515126 doi:http://dx.doi.org/10.1038/s41467-018-03412-8
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