Open AccessPlant Endocytosis Requires the ER Membrane-Anchored Proteins VAP27-1 and VAP27-3
Author(s) -
Giovanni Stefano,
Luciana Renna,
Clarissa Wormsbaecher,
Jessie Gamble,
Krzysztof Zienkiewicz,
Federica Brandizzí
Publication year - 2018
Publication title -
cell reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.264
H-Index - 154
eISSN - 2639-1856
pISSN - 2211-1247
DOI - 10.1016/j.celrep.2018.04.091
Subject(s) - endocytic cycle , endocytosis , endosome , clathrin , endoplasmic reticulum , microbiology and biotechnology , receptor mediated endocytosis , membrane contact site , membrane , clathrin adaptor proteins , chemistry , membrane protein , biology , biochemistry , integral membrane protein , receptor , intracellular
Through yet-undefined mechanisms, the plant endoplasmic reticulum (ER) has a critical role in endocytosis. The plant ER establishes a close association with endosomes and contacts the plasma membrane (PM) at ER-PM contact sites (EPCSs) demarcated by the ER membrane-associated VAMP-associated-proteins (VAP). Here, we investigated two plant VAPs, VAP27-1 and VAP27-3, and found an interaction with clathrin and a requirement for the homeostasis of clathrin dynamics at endocytic membranes and endocytosis. We also demonstrated direct interaction of VAP27-proteins with phosphatidylinositol-phosphate lipids (PIPs) that populate endocytic membranes. These results support that, through interaction with PIPs, VAP27-proteins bridge the ER with endocytic membranes and maintain endocytic traffic, likely through their interaction with clathrin.
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