UV-radiation-induced internalization of the epidermal growth factor receptor requires distinct serine and tyrosine residues in the cytoplasmic carboxy-terminal domain.

Oksvold, MP, Thien, CBF, Widerberg, J, Chantry, A, Huitfeldt, HS and Langdon, WY (2004) UV-radiation-induced internalization of the epidermal growth factor receptor requires distinct serine and tyrosine residues in the cytoplasmic carboxy-terminal domain. Radiation Research, 161 (6). pp. 685-691. ISSN 1938-5404

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Abstract

The mechanism of UV-radiation-induced EGF receptor (EGFR) internalization remains to be established. In the present study, we found UV-radiation-mediated internalization of the EGFR to be dependent on the cytoplasmic carboxy-terminal region. UV radiation was unable to induce internalization of EGFR carboxy-terminal truncation mutants where all or four of the five major autophosphorylation sites were missing (963- and 1028-EGFR, respectively). Mutational removal of serine residues 1046, 1047, 1057 and 1142 within the carboxy-terminal receptor region was also sufficient to abolish UV-radiation-induced internalization of the EGFR. Furthermore, the UV-radiation-induced internalization was abrogated for an EGFR mutated in tyrosine 1045 (Y1045F), the major c-Cbl binding site. However, UV radiation did not induce phosphorylation at tyrosine 1045, in contrast to the prominent phosphorylation induced by EGF. Our results suggest a mechanism for UV-radiation-induced internalization of EGFR involving a conformational change that is dependent on structural elements formed by specific serine and tyrosine residues in the carboxy-terminal domain.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
Related URLs:
Depositing User: EPrints Services
Date Deposited: 01 Oct 2010 13:37
Last Modified: 24 Jul 2019 16:46
URI: https://ueaeprints.uea.ac.uk/id/eprint/793
DOI: 10.1667/RR3185

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