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bioRxiv · 10.1101/2022.01.07.475403

SH3Ps recruit auxilin-like vesicle uncoating factors into clathrin-mediated endocytosis

Adamowski, M.·Matijevic, I.·Narasimhan, M.·Friml, J.
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Abstract

Clathrin-mediated endocytosis (CME) is an essential process of cellular cargo uptake operating in all eukaryotes. In animal and yeast, CME involves BAR-SH3 domain proteins, endophilins and amphiphysins, which function at the conclusion of CME to recruit factors for vesicle scission and uncoating. Arabidopsis thaliana contains BAR-SH3 domain proteins SH3P1-3, but their role is poorly understood. We identify SH3P1-3 as functional homologues of endophilin/amphiphysin. SH3P1-3 bind to discrete foci at the plasma membrane (PM), and colocalization indicates late recruitment of SH3P2 to a subset of clathrin-coated pits. PM recruitment pattern of SH3P2 is nearly identical to its interactor, a putative vesicle uncoating factor AUXILIN-LIKE1, and SH3P1-3 are required for most of AUXILIN-LIKE1 PM binding. This indicates a plant-specific modification of CME, where BAR-SH3 proteins recruit auxilin-like uncoating factors, rather than the uncoating phosphatases synaptojanins. Furthermore, we identify an unexpected redundancy between SH3P1-3 and a plant-specific endocytic adaptor, TPLATE complex, showing a contribution of SH3P1-3 to gross CME.

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Adamowski, M., Matijevic, I., Narasimhan, M., Friml, J.. 2022-01-09. SH3Ps recruit auxilin-like vesicle uncoating factors into clathrin-mediated endocytosis. https://doi.org/10.1101/2022.01.07.475403

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