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

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 inter- action 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

Authors:
 [1];  [1];  [2];  [1];  [3];  [1]
  1. Michigan State Univ., East Lansing, MI (United States)
  2. Michigan State Univ., East Lansing, MI (United States); The Ohio State Univ., Columbus, OH (United States)
  3. Michigan State Univ., East Lansing, MI (United States); Georg-August-University, Gottingen (Germany)
Publication Date:
Research Org.:
Michigan State Univ., East Lansing, MI (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1504935
Grant/Contract Number:  
[FG02-91ER20021]
Resource Type:
Accepted Manuscript
Journal Name:
Cell Reports
Additional Journal Information:
[ Journal Volume: 23; Journal Issue: 8]; Journal ID: ISSN 2211-1247
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; endosplasmic reticulum; endocytosis; clathrin; trans-golgi network; ER-PM contact sites

Citation Formats

Stefano, Giovanni, Renna, Luciana, Wormsbaecher, Clarissa, Gamble, Jessie, Zienkiewicz, Krzysztof, and Brandizzi, Federica. Plant Endocytosis Requires the ER Membrane-Anchored Proteins VAP27-1 and VAP27-3. United States: N. p., 2018. Web. doi:10.1016/j.celrep.2018.04.091.
Stefano, Giovanni, Renna, Luciana, Wormsbaecher, Clarissa, Gamble, Jessie, Zienkiewicz, Krzysztof, & Brandizzi, Federica. Plant Endocytosis Requires the ER Membrane-Anchored Proteins VAP27-1 and VAP27-3. United States. doi:10.1016/j.celrep.2018.04.091.
Stefano, Giovanni, Renna, Luciana, Wormsbaecher, Clarissa, Gamble, Jessie, Zienkiewicz, Krzysztof, and Brandizzi, Federica. Tue . "Plant Endocytosis Requires the ER Membrane-Anchored Proteins VAP27-1 and VAP27-3". United States. doi:10.1016/j.celrep.2018.04.091. https://www.osti.gov/servlets/purl/1504935.
@article{osti_1504935,
title = {Plant Endocytosis Requires the ER Membrane-Anchored Proteins VAP27-1 and VAP27-3},
author = {Stefano, Giovanni and Renna, Luciana and Wormsbaecher, Clarissa and Gamble, Jessie and Zienkiewicz, Krzysztof and Brandizzi, Federica},
abstractNote = {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 inter- action 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},
doi = {10.1016/j.celrep.2018.04.091},
journal = {Cell Reports},
number = [8],
volume = [23],
place = {United States},
year = {2018},
month = {5}
}

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Cited by: 7 works
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Figures / Tables:

Figure 1 Figure 1: VAP27-1 and VAP27-3 Interact with Clathrin and Bind Lipids Abundant in Endocytic Membranes (A) List of proteins and heatmap of the number of peptides detected by coIP experiments for VAP27-1-YFP and VAP27-3-YFP (0 indicates absence of peptides). (B) Y2H assay of the VAP27-cytosolic domain with five ofmore » the clathrin proteins identified in the pulldowns (blue color: protein-protein interaction). (C) Percentage (%) of blue color intensity (relative to B) compared to the positive control (spot 12 in B showing the degree of protein interaction). (D) Protein-lipid overlay assay.« less

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