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TitleCryo-EM structure of soluble VPS13C suggests its regulation by a conformational switch and by calmodulin.
Journal, issue, pagesMol Cell, Vol. 86, Issue 14, Page 2843-2857.e10, Year 2026
Publish dateJul 7, 2026
AuthorsDazhi Li / Xinbo Wang / Hongyan Hao / Jessica Eden / Bodan Hu / Emma E Walsh / Matthew A H Parson / Stephanie Hamill / Yuting Li / Guochao Chen / John E Burke / Pietro De Camilli / Karin M Reinisch /
PubMed AbstractBridge-like lipid transfer proteins (BLTPs) play fundamental roles in cellular lipid redistribution between organellar membranes. They comprise bridge domains spanning organelles at contact sites ...Bridge-like lipid transfer proteins (BLTPs) play fundamental roles in cellular lipid redistribution between organellar membranes. They comprise bridge domains spanning organelles at contact sites that allow lipids to transit through the cytosol between adjacent membranes. The assembly of BLTPs into complexes with adaptor proteins enables lipid transfer. To address the mechanisms underlying the assembly and regulation of BLTP complexes, we used cryo-EM to resolve the structure of one such BLTP, the Parkinson's disease protein VPS13C, at near-atomic resolution. The structure identifies a lipid-transfer-nonpermissive conformation, in which the built-in C-terminal VAB adaptor module blocks the end of the lipid transfer bridge, interfering with lipid delivery. We also identify calmodulin (CaM), central to calcium signaling, as a constitutive VPS13C interactor. Calcium induces conformational changes in the VPS13C-CaM complex, suggesting calcium regulation of VPS13 function. Altogether, this structure of intact VPS13C serves as a starting point for understanding its regulation and that of other VPS13 proteins.
External linksMol Cell / PubMed:42413490
MethodsEM (single particle)
Resolution3.75 - 4.2 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

EMDB-73345: Consensus map of full-length human VPS13C in complex with calmodulin
Method: EM (single particle) / Resolution: 4.2 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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