Via Proteins and Lipids - Versatility of VAPs at Dynamic Membrane Contact Sites.

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?