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• W2138430231 abstract "A variety of studies have implicated the lipid PtdIns(4,5)P 2 in endocytic internalization, but how this lipid mediates its effects is not known. The AP180 N-terminal homology (ANTH) domain is a PtdIns(4,5)P 2 -binding module found in several proteins that participate in receptor-mediated endocytosis. One such protein is yeast Sla2p, a highly conserved actin-binding protein essential for actin organization and endocytic internalization. To better understand how PtdIns(4,5)P 2 binding regulates actin-dependent endocytosis, we investigated the functions of Sla2p's ANTH domain. A liposome-binding assay revealed that Sla2p binds to PtdIns(4,5)P 2 specifically through its ANTH domain and identified specific lysine residues required for this interaction. Mutants of Sla2p deficient in PtdIns(4,5)P 2 binding showed significant defects in cell growth, actin organization, and endocytic internalization. These defects could be rescued by increasing PtdIns(4,5)P 2 levels in vivo. Strikingly, mutant Sla2p defective in PtdIns(4,5)P 2 binding localized with the endocytic machinery at the cell cortex, establishing that the ANTH-PtdIns(4,5)P 2 interaction is not necessary for this association. In contrast, multicolor real-time fluorescence microscopy and particle-tracking analysis demonstrated that PtdIns(4,5)P 2 binding is required during endocytic internalization. These results demonstrate that the interaction of Sla2p's ANTH domain with PtdIns(4,5)P 2 plays a key role in regulation of the dynamics of actin-dependent endocytic internalization." @default.
• W2138430231 created "2016-06-24" @default.
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• W2138430231 date "2005-02-01" @default.
• W2138430231 modified "2023-09-29" @default.
• W2138430231 title "Interaction of Sla2p's ANTH Domain with PtdIns(4,5)P₂Is Important for Actin-dependent Endocytic Internalization" @default.
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• W2138430231 doi "https://doi.org/10.1091/mbc.e04-08-0740" @default.
• W2138430231 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/545906" @default.
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