Regulatory interactions in the recognition of endocytic sorting signals by AP-2 complexes

The EMBO Journal
I RapoportT Kirchhausen

Abstract

Many plasma membrane proteins destined for endocytosis are concentrated into clathrin-coated pits through the recognition of a tyrosine-based motif in their cytosolic domains by an adaptor (AP-2) complex. The mu2 subunit of isolated AP-2 complexes binds specifically, but rather weakly, to proteins bearing the tyrosine-based signal. We now demonstrate, using peptides with a photoreactive probe, that this binding is strengthened significantly when the AP-2 complex is present in clathrin coats, indicating that there is cooperativity between receptor-AP-2 interactions and coat formation. Phosphoinositides with a phosphate at the D-3 position of the inositol ring, but not other isomers, also increase the affinity of the AP-2 complex for the tyrosine-based motif. AP-2 is the first protein known (in any context) to interact with phosphatidylinositol 3-phosphate. Our findings indicate that receptor recruitment can be coupled to clathrin coat assembly and suggest a mechanism for regulation of membrane traffic by lipid products of phosphoinositide 3-kinases.

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Citations

Sep 3, 1999·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·R HeilkerP Crottet
Jul 13, 2001·European Journal of Immunology·H SchneiderC E Rudd
Jun 8, 1999·Chemistry and Physics of Lipids·J M GaullierH Stenmark
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May 18, 2004·Proceedings of the National Academy of Sciences of the United States of America·Markus R Wenk, Pietro De Camilli

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