The AP-2 adaptor β2 appendage scaffolds alternate cargo endocytosis

Peter Keyel, James R Thieman, Robyn Roth, E Erkan, E T Everett, Simon C Watkins, John E Heuser, Linton M Traub

Research output: Contribution to journalArticle

Abstract

The independently folded appendages of the large α and β2 subunits of the endocytic adaptor protein (AP)-2 complex coordinate proper assembly and operation of endocytic components during clathrin-mediated endocytosis. The β2 subunit appendage contains a common binding site for β-arrestin or the autosomal recessive hypercholesterolemia (ARH) protein. To determine the importance of this interaction surface in living cells, we used small interfering RNA-based gene silencing. The effect of extinguishing β2 subunit expression on the internalization of transferrin is considerably weaker than an AP-2 α subunit knockdown. We show the mild sorting defect is due to fortuitous substitution of the β2 chain with the closely related endogenous β1 subunit of the AP-1 adaptor complex. Simultaneous silencing of both β1 and β2 subunit transcripts recapitulates the strong α subunit RNA interference (RNAi) phenotype and results in loss of ARH from endocytic clathrin coats. An RNAi-insensitive β2-yellow f
Original languageEnglish
Pages (from-to)5309-5326
JournalMolecular Biology of the Cell
StatePublished - 2008

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