SH3Ps recruit auxilin-like vesicle uncoating factors for clathrin-mediated endocytosis.
Autor: | Adamowski M; Institute of Science and Technology Austria, Am Campus 1, 3400 Klosterneuburg, Austria; Plant Breeding and Acclimatization Institute - National Research Institute, Radzików, 05-870 Błonie, Poland., Randuch M; Institute of Science and Technology Austria, Am Campus 1, 3400 Klosterneuburg, Austria., Matijević I; Institute of Science and Technology Austria, Am Campus 1, 3400 Klosterneuburg, Austria., Narasimhan M; Institute of Science and Technology Austria, Am Campus 1, 3400 Klosterneuburg, Austria., Friml J; Institute of Science and Technology Austria, Am Campus 1, 3400 Klosterneuburg, Austria. Electronic address: jiri.friml@ist.ac.at. |
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Jazyk: | angličtina |
Zdroj: | Cell reports [Cell Rep] 2024 May 28; Vol. 43 (5), pp. 114195. Date of Electronic Publication: 2024 May 07. |
DOI: | 10.1016/j.celrep.2024.114195 |
Abstrakt: | Clathrin-mediated endocytosis (CME) is an essential process of cargo uptake operating in all eukaryotes. In animals and yeast, BAR-SH3 domain proteins, endophilins and amphiphysins, function at the conclusion of CME to recruit factors for vesicle scission and uncoating. Arabidopsis thaliana contains the BAR-SH3 domain proteins SH3P1-SH3P3, but their role is poorly understood. Here, we identify SH3Ps as functional homologs of endophilin/amphiphysin. SH3P1-SH3P3 bind to discrete foci at the plasma membrane (PM), and SH3P2 recruits late to a subset of clathrin-coated pits. The SH3P2 PM recruitment pattern is nearly identical to its interactor, a putative uncoating factor, AUXILIN-LIKE1. Notably, SH3P1-SH3P3 are required for most of AUXILIN-LIKE1 recruitment to the PM. This indicates a plant-specific modification of CME, where BAR-SH3 proteins recruit auxilin-like uncoating factors rather than the uncoating phosphatases, synaptojanins. SH3P1-SH3P3 act redundantly in overall CME with the plant-specific endocytic adaptor TPLATE complex but not due to an SH3 domain in its TASH3 subunit. Competing Interests: Declaration of interests The authors declare no competing interests. (Copyright © 2024 The Author(s). Published by Elsevier Inc. All rights reserved.) |
Databáze: | MEDLINE |
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