7fad: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7fad]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] and [https://en.wikipedia.org/wiki/Xenopus_tropicalis Xenopus tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FAD FirstGlance]. <br> | <table><tr><td colspan='2'>[[7fad]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] and [https://en.wikipedia.org/wiki/Xenopus_tropicalis Xenopus tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FAD FirstGlance]. <br> | ||
</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=7fad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fad OCA], [https://pdbe.org/7fad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fad RCSB], [https://www.ebi.ac.uk/pdbsum/7fad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fad ProSAT]</span></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]] 3.204Å</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=7fad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fad OCA], [https://pdbe.org/7fad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fad RCSB], [https://www.ebi.ac.uk/pdbsum/7fad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fad ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q6DDJ4_XENLA Q6DDJ4_XENLA] Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.[RuleBase:RU363050] | [https://www.uniprot.org/uniprot/Q6DDJ4_XENLA Q6DDJ4_XENLA] Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.[RuleBase:RU363050] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The primary cilium, a microtubule-based sensory organelle, undergoes cycles of assembly and disassembly that govern the cell cycle progression critical to cell proliferation and differentiation. Although cilia assembly has been studied extensively, the molecular mechanisms underlying cilia disassembly are less well understood. Here, we uncover a gamma-tubulin ring complex (gamma-TuRC)-dependent pathway that promotes cilia disassembly and thereby prevents cilia formation. We further demonstrate that Kif2A, a kinesin motor that bears microtubule-depolymerizing activity, is recruited to the cilium basal body in a gamma-TuRC-dependent manner. Our mechanistic analyses show that gamma-TuRC specifically recruits Kif2A via the GCP2 subunit and its binding partner Mzt2. Hence, despite the long-standing view that gamma-TuRC acts mainly as a microtubule template, we illustrate that its functional heterogeneity at the basal body facilitates both microtubule nucleation and Kif2A recruitment-mediated regulation of ciliogenesis, ensuring cell cycle progression. | |||
Alpha gamma-tubulin complex-dependent pathway suppresses ciliogenesis by promoting cilia disassembly.,Shankar S, Hsu ZT, Ezquerra A, Li CC, Huang TL, Coyaud E, Viais R, Grauffel C, Raught B, Lim C, Luders J, Tsai SY, Hsia KC Cell Rep. 2022 Nov 15;41(7):111642. doi: 10.1016/j.celrep.2022.111642. PMID:36384111<ref>PMID:36384111</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7fad" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Tubulin 3D Structures|Tubulin 3D Structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 22:34, 29 May 2024
Crystal structure of Xenopus GCP2-N terminal domain and Mzt2Crystal structure of Xenopus GCP2-N terminal domain and Mzt2
Structural highlights
FunctionQ6DDJ4_XENLA Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.[RuleBase:RU363050] Publication Abstract from PubMedThe primary cilium, a microtubule-based sensory organelle, undergoes cycles of assembly and disassembly that govern the cell cycle progression critical to cell proliferation and differentiation. Although cilia assembly has been studied extensively, the molecular mechanisms underlying cilia disassembly are less well understood. Here, we uncover a gamma-tubulin ring complex (gamma-TuRC)-dependent pathway that promotes cilia disassembly and thereby prevents cilia formation. We further demonstrate that Kif2A, a kinesin motor that bears microtubule-depolymerizing activity, is recruited to the cilium basal body in a gamma-TuRC-dependent manner. Our mechanistic analyses show that gamma-TuRC specifically recruits Kif2A via the GCP2 subunit and its binding partner Mzt2. Hence, despite the long-standing view that gamma-TuRC acts mainly as a microtubule template, we illustrate that its functional heterogeneity at the basal body facilitates both microtubule nucleation and Kif2A recruitment-mediated regulation of ciliogenesis, ensuring cell cycle progression. Alpha gamma-tubulin complex-dependent pathway suppresses ciliogenesis by promoting cilia disassembly.,Shankar S, Hsu ZT, Ezquerra A, Li CC, Huang TL, Coyaud E, Viais R, Grauffel C, Raught B, Lim C, Luders J, Tsai SY, Hsia KC Cell Rep. 2022 Nov 15;41(7):111642. doi: 10.1016/j.celrep.2022.111642. PMID:36384111[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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