View source for 9yqq


==Cryo-EM structure of the VPS13C C-terminal region==
<StructureSection load='9yqq' size='340' side='right'caption='[[9yqq]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9yqq]] is a 1 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=9YQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9YQQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</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=9yqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9yqq OCA], [https://pdbe.org/9yqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9yqq RCSB], [https://www.ebi.ac.uk/pdbsum/9yqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9yqq ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/VP13C_HUMAN VP13C_HUMAN] Young-onset Parkinson disease. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/VP13C_HUMAN VP13C_HUMAN] Mediates the transfer of lipids between membranes at organelle contact sites (By similarity). Necessary for proper mitochondrial function and maintenance of mitochondrial transmembrane potential (PubMed:26942284). Involved in the regulation of PINK1/PRKN-mediated mitophagy in response to mitochondrial depolarization (PubMed:26942284).[UniProtKB:Q07878]<ref>PMID:26942284</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bridge-like lipid transfer proteins (BLTPs) play central roles in redistributing lipids from their primary site of synthesis in the endoplasmic reticulum to other organelles. They comprise bridge-domains spanning between organelles at contact sites that allow lipids to transit the cytosol between adjacent membranes. The assembly of BLTPs into complexes with adaptor proteins enables their lipid transfer ability. To address the mechanisms underlying assembly and regulation of BLTP complexes, we used cryo-EM to resolve the structure of one such BLTP, the Parkinson's protein VPS13C, at near-atomic resolution. The structure identifies a lipid-transfer-nonpermissive conformation, where the built-in C-terminal VAB adaptor module blocks the end of the lipid transfer bridge, interfering with lipid delivery. We also identify calmodulin, central to calcium signaling, as a VPS13 partner, suggesting calcium regulation of VPS13 function. Altogether, this structure of intact VPS13C serves as starting point to understand its regulation and, more broadly, that of other BLTPs.

Insights into the regulation of VPS13 family bridge-like lipid transfer proteins from the structure of VPS13C.,Li D, Wang X, Hu B, Hao H, Hamill S, Li Y, Chen G, De Camilli P, Reinisch KM bioRxiv [Preprint]. 2025 Nov 11:2025.11.10.687702. doi: , 10.1101/2025.11.10.687702. PMID:41292763<ref>PMID:41292763</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9yqq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Li D]]
[[Category: Reinisch KM]]