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Updated: Sep 9, 2025

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics
Published on: September 2, 2020
Via Proteins and Lipids - Versatility of VAPs at Dynamic Membrane Contact Sites
Dan Zhang1,2
1Temasek Life Sciences Laboratory, National University of Singapore, Singapore, Singapore.
Abstract:
VAMP-associated proteins (VAPs) are highly conserved, endoplasmic reticulum (ER)-resident receptors that tether the ER to various membrane compartments in eukaryotic cells. Each VAP contains a transmembrane helix at its extreme C-terminus and a conserved N-terminal major sperm protein (MSP) domain that mediates various cytosolic interactions via both protein and lipid binding. Here, I question the fundamental difference between protein- and lipid-based associations in VAP-driven membrane contact site (MCS) formation and function - could the lipid affinity of VAPs be an overlooked factor in MCS dynamic regulation?
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