RT Journal Article
SR Electronic
T1 SH3Ps recruit auxilin-like vesicle uncoating factors into clathrin-mediated endocytosis
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2022.01.07.475403
DO 10.1101/2022.01.07.475403
A1 Maciek Adamowski
A1 Ivana Matijević
A1 Madhumitha Narasimhan
A1 Jiří Friml
YR 2022
UL http://biorxiv.org/content/early/2022/01/09/2022.01.07.475403.abstract
AB 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.Competing Interest StatementThe authors have declared no competing interest.