ORP/Osh mediate cross-talk between ER-plasma membrane contact site components and plasma membrane SNAREs

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Weber-Boyvat , M , Trimbuch , T , Shah , S , Jäntti , J , Olkkonen , V M & Rosenmund , C 2021 , ' ORP/Osh mediate cross-talk between ER-plasma membrane contact site components and plasma membrane SNAREs ' , Cellular and Molecular Life Sciences , vol. 78 , pp. 1689-1708 . https://doi.org/10.1007/s00018-020-03604-w

Title: ORP/Osh mediate cross-talk between ER-plasma membrane contact site components and plasma membrane SNAREs
Author: Weber-Boyvat, Marion; Trimbuch, Thorsten; Shah, Saundarya; Jäntti, Jussi; Olkkonen, Vesa M.; Rosenmund, Christian
Contributor: University of Helsinki, Medicum
Date: 2021-02
Language: eng
Number of pages: 20
Belongs to series: Cellular and Molecular Life Sciences
ISSN: 1420-682X
URI: http://hdl.handle.net/10138/333095
Abstract: OSBP-homologous proteins (ORPs, Oshp) are lipid binding/transfer proteins. Several ORP/Oshp localize to membrane contacts between the endoplasmic reticulum (ER) and the plasma membrane, where they mediate lipid transfer or regulate lipid-modifying enzymes. A common way in which they target contacts is by binding to the ER proteins, VAP/Scs2p, while the second membrane is targeted by other interactions with lipids or proteins. We have studied the cross-talk of secretory SNARE proteins and their regulators with ORP/Oshp and VAPA/Scs2p at ER-plasma membrane contact sites in yeast and murine primary neurons. We show that Oshp-Scs2p interactions depend on intact secretory SNARE proteins, especially Sec9p. SNAP-25/Sec9p directly interact with ORP/Osh proteins and their disruption destabilized the ORP/Osh proteins, associated with dysfunction of VAPA/Scs2p. DeletingOSH1-3in yeast or knocking down ORP2 in primary neurons reduced the oligomerization of VAPA/Scs2p and affected their multiple interactions with SNAREs. These observations reveal a novel cross-talk between the machineries of ER-plasma membrane contact sites and those driving exocytosis.
Subject: Osh
Sec9
ORP
SNAP-25
SNARE
Membrane contact site
OXYSTEROL-BINDING-PROTEIN
ENDOPLASMIC-RETICULUM
FFAT MOTIF
HOMOLOG
COMPLEX
REVEALS
GOLGI
VAP
TRANSPORT
FUSION
1182 Biochemistry, cell and molecular biology
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