Journal article

DIFFERENTIAL INVITRO PHOSPHORYLATION OF CLATHRIN LIGHT-CHAINS BY THE EPIDERMAL GROWTH-FACTOR RECEPTOR-ASSOCIATED PROTEIN TYROSINE KINASE AND A PP60C-SRC-RELATED SPLEEN TYROSINE KINASE

MJ MOOIBROEK, HC CHENG, JH WANG

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS | Published : 1992

Abstract

The epidermal growth factor (EGF) receptor-associated protein tyrosine kinase activity has been suggested to play important roles in the EGF-enhanced, clathrin-coated pit-mediated receptor internalization (W. S. Chen, C. S. Lazar, M. Peonie, R. Y. Tsien, G. N. Gill, and M. G. Rosenfeld, 1987, Nature 328, 820-823) but the kinase substrate important for this process has not been identified. This study demonstrates that the EGF receptor, partially purified from A431 epidermoid carcinoma cells, catalyzes the phosphorylation of one of the two clathrin light chains, clathrin light chain a (LCa). The phosphorylation activity is stimulated by EGF and immunoprecipitated by an EGF receptor monoclonal ..

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