Proteomics

Dataset Information

0

HDX-MS Analysis of VPS13C-dATG2C-3xFLAG-CaM +/- Calcium


ABSTRACT: We carried out HDX-MS experiments on two conditions, VPS13C(dATG2C)-3xFLAG + EGTA, and VPS13C(dATG2C)-3xFLAG + Ca2+ to define conformational changes accompanying Ca2+. We saw an overall 69.7% coverage of VPS13C(dATG2C)-3xFLAG with 424 peptides identified and 66.4% coverage of CaM with 16 peptides identified. Looking at VPS13C(dATG2C)-3xFLAG, there is an exposure from 135-142 upon the addition of Ca2+. In CaM, there is an exposure from 73-85, and protections are seen at 91-103 and 125-141 upon the addition of Ca2+.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke  

LAB HEAD: John Burke

PROVIDER: PXD076522 | Pride | 2026-06-02

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
01_22_26_165_EW_PM4_MSMS.d.zip Other
03_18_26_054_EW13_VPS13C-dATG2C_CaM_42min_MSMS.d.zip Other
CaM_FASTA.txt Txt
EW13_VPS13C-dATG2C-3xFLAG-CaM_42min_peptides.csv Csv
EWHDX13_CaM.hdx Other
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Publications

Insights into the regulation of VPS13 family bridge-like lipid transfer proteins from the structure of VPS13C.

Li Dazhi D   Wang Xinbo X   Hu Bodan B   Hao Hongyan H   Hamill Stephanie S   Li Yuting Y   Chen Guochao G   De Camilli Pietro P   Reinisch Karin M KM  

bioRxiv : the preprint server for biology 20251111


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 us  ...[more]

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