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NDF/heregulin stimulates the phosphorylation of Her3/erbB3
Author(s) -
Kita Yoshiko A.,
Barff Jenny,
Luo Yi,
Wen Duanzhi,
Brankow David,
Hu Sylvia,
Liu Naili,
Prigent Sally A.,
Gullick William J.,
Nicolson Margery
Publication year - 1994
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 - 10.1016/0014-5793(94)00644-x
Subject(s) - erbb3 , neuregulin , phosphorylation , chemistry , neuregulin 1 , microbiology and biotechnology , receptor , biology , biochemistry , receptor tyrosine kinase
Her3/erbB3 has been identified as a third member of the epidermal growth factor receptor (EGFR) family [(1989) Proc. Natl. Acad. Sci. USA 86, 9193–9197; (1990) Proc. Natl. Acad. Sci. USA 87, 4905–4909]. The natural ligand for Her3 has not been identified. Although recently NDF has been proposed as a specific ligand for Her4 [(1993) Nature 366, 473–475; (1993) J. Biol. Chem. 268, 18407–18410], we report here that Her3 was phosphorylated on tyrosine not only in three breast carcinoma cell lines, MDAMB453, MDAMB468 and SKBR3, but also in Her3‐transfected CHO cells in response to NDF stimulation. In further studies, cells were reacted with 125 I‐labeled NDF and then chemically crosslinked. Immunoprecipitation with anti‐Her3 revealed a dense high M W band, greater than 400 kDa. The results suggest that NDF may be a ligand of Her3 and induces receptor hetero‐oligomerization.