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. Stefano et al. demonstrate that plant VAPs (VAP27-1 and VAP27-3) interact with clathrin and with phosphatidylinositol-phosphate lipids (PIPs) that populate endocytic membranes. The findings support a model showing that, through interaction with PIPs and clathrin, VAP27-proteins bridge the ER with endocytic membranes and maintain endocytic traffic.

Plant Endocytosis Requires the ER Membrane-Anchored Proteins VAP27-1 and VAP27-3 / Stefano G.; Renna L.; Wormsbaecher C.; Gamble J.; Zienkiewicz K.; Brandizzi F.. - In: CELL REPORTS. - ISSN 2211-1247. - ELETTRONICO. - 23:(2018), pp. 2299-2307. [10.1016/j.celrep.2018.04.091]

Plant Endocytosis Requires the ER Membrane-Anchored Proteins VAP27-1 and VAP27-3

Stefano G.;Renna L.;
2018

Abstract

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. Stefano et al. demonstrate that plant VAPs (VAP27-1 and VAP27-3) interact with clathrin and with phosphatidylinositol-phosphate lipids (PIPs) that populate endocytic membranes. The findings support a model showing that, through interaction with PIPs and clathrin, VAP27-proteins bridge the ER with endocytic membranes and maintain endocytic traffic.
2018
23
2299
2307
Goal 3: Good health and well-being for people
Stefano G.; Renna L.; Wormsbaecher C.; Gamble J.; Zienkiewicz K.; Brandizzi F.
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1209435
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