Specific association of annexin 1 with plasma membrane‐resident and internalized EGF receptors mediated through the protein core domain | Zendy

Radke Susanne | Zendy; Austermann Judith | Zendy; Russo-Marie Francoise | Zendy; Gerke Volker | Zendy; Rescher Ursula | Zendy

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Specific association of annexin 1 with plasma membrane‐resident and internalized EGF receptors mediated through the protein core domain

Author(s) -

Radke Susanne,

Austermann Judith,

Russo-Marie Francoise,

Gerke Volker,

Rescher Ursula

Publication year - 2004

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2004.10.078

Subject(s) - annexin a2 , internalization , microbiology and biotechnology , phosphorylation , epidermal growth factor , receptor , tyrosine phosphorylation , receptor tyrosine kinase , immunoprecipitation , tyrosine kinase , annexin , chemistry , mediator , biology , biochemistry , cell , gene

Phosphorylation of the Ca 2+ and membrane‐binding protein annexin 1 by epidermal growth factor (EGF) receptor tyrosine kinase has been thought to be involved in regulation of the EGF receptor trafficking. To elucidate the interaction of annexin 1 during EGF receptor internalization, we followed the distribution of annexin 1‐GFP fusion proteins at sites of internalizing EGF receptors. The observed association of annexin 1 with EGF receptors was confirmed by immunoprecipitation. We found that this interaction was independent of a functional phosphorylation site in the annexin 1 N‐terminal domain but mediated through the Ca 2+ binding core domain.

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