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VAP-mediated membrane tethering mechanisms implicate ER-PM contact function in pH homeostasis

ABSTRACT: MS analyses of interactome of full-length (i.e., Scs2 and Scs22) and TM-truncated (i.e., Scs2N and Scs22N) fission yeast VAPs.

ORGANISM(S): Schizosaccharomyces Pombe (fission Yeast)

SUBMITTER: Dan Zhang

PROVIDER: PXD053887 | JPOST Repository | Fri Aug 09 00:00:00 BST 2024

REPOSITORIES: jPOST

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			Action	DRS
	GFP%20control%20interactome_whole%20IP%20solution_replicate%203_RAW.zip	Other
	GFP%20control_replicate%203_230619_2306S07_344__FDR.xlsx	Xlsx
	Scs2%20interactome_mutiple%20gel%20slices_replicate%201_RAW.zip	Other
	Scs2%20interactome_mutiple%20gel%20slices_replicate%201_Results.zip	Other
	Scs2%20interactome_whole%20IP%20solution_replicate%202_RAW.zip	Other

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Publications

VAP-mediated membrane-tethering mechanisms implicate ER-PM contact function in pH homeostasis.

Hoh Kar Ling KL Mu Baicong B See Tingyi T Ng Amanda Yunn Ee AYE Ng Annabel Qi En AQE Zhang Dan D

Cell reports 20240806 8

Vesicle-associated membrane protein (VAMP)-associated proteins (VAPs) are highly conserved endoplasmic reticulum (ER)-resident proteins that establish ER contacts with multiple membrane compartments in many eukaryotes. However, VAP-mediated membrane-tethering mechanisms remain ambiguous. Here, focusing on fission yeast ER-plasma membrane (PM) contact formation, using systematic interactome analyses and quantitative microscopy, we predict a non-VAP-protein direct binding-based ER-PM coupling. We ...[more]

PMID: 39110593

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