Structure of an arrestin2-clathrin complex reveals a novel clathrin binding domain that modulates receptor trafficking.

ABSTRACT: Non-visual arrestins play a pivotal role as adaptor proteins in regulating the signaling and trafficking of multiple classes of receptors. Although arrestin interaction with clathrin, AP-2, and phosphoinositides contributes to receptor trafficking, little is known about the configuration and dynamics of these interactions. Here, we identify a novel interface between arrestin2 and clathrin through x-ray diffraction analysis. The intrinsically disordered clathrin binding box of arrestin2 interacts with a groove between blades 1 and 2 in the clathrin beta-propeller domain, whereas an 8-amino acid splice loop found solely in the long isoform of arrestin2 (arrestin2L) interacts with a binding pocket formed by blades 4 and 5 in clathrin. The apposition of the two binding sites in arrestin2L sugg

SUBMITTER: Kang DS 

PROVIDER: S-EPMC2785616 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature