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TitleInsights into the regulation of VPS13 family bridge-like lipid transfer proteins from the structure of VPS13C.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateNov 11, 2025
AuthorsDazhi Li / Xinbo Wang / Bodan Hu / Hongyan Hao / Stephanie Hamill / Yuting Li / Guochao Chen / Pietro De Camilli / Karin M Reinisch /
PubMed AbstractBridge-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- ...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.
External linksbioRxiv / PubMed:41292763 / PubMed Central
MethodsEM (single particle)
Resolution3.75 - 4.13 Å
Structure data

73343

9yqp

EMDB-73343, PDB-9yqp:
Cryo-EM structure of the VPS13C N-terminal region in complex with Calmodulin
Method: EM (single particle) / Resolution: 4.1 Å

73344

9yqq

EMDB-73344, PDB-9yqq:
Cryo-EM structure of the VPS13C C-terminal region
Method: EM (single particle) / Resolution: 3.8 Å

73373

9yrp

EMDB-73373, PDB-9yrp:
Full-length human VPS13C in complex with calmodulin from the CryoEM composite map
Method: EM (single particle) / Resolution: 4.13 Å

PDB-9yrm:
CryoEM Structure of VPS13 protein, 1-1390 from C. thermophilum, in complex with calmodulin
Method: ELECTRON MICROSCOPY / Resolution: 3.75 Å

Source
  • homo sapiens (human)
  • thermochaetoides thermophila (fungus)
KeywordsLIPID TRANSPORT / Lipid transport protein; BLTP; membrane repair; membrane homeostasis; VPS13C / lipid transport protein; BLTP / Lipid Transport protein; BLTP; lysosomal membrane repair; membrane homeostasis

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