Tyrosine phosphorylation of the beta2 subunit of clathrin adaptor complex AP-2 reveals the role of a di-leucine motif in the epidermal growth factor receptor trafficking.

Abstract excerpt

Tyrosine phosphorylation of the beta2 subunit of clathrin adaptor complex AP-2 was detected in three types of cells treated with epidermal growth factor (EGF). The tyrosine phosphorylation was observed during recruitment of EGF receptors into coated pits at 4 degrees C and reached maximum at 37 degrees C at post-recruitment stages of endocytosis. An inhibitor of EGF receptor kinase completely abolished this...

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