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By digestion of the receptor with endoglycosidase F it was shown that an altered pattern of glycosylation could not account for the smaller size of the protein, although it could explain the appearance of the CHO 11 receptor as a doublet protein. A deletion was located to the transfected cDNA and shown to involve the removal of coding sequences for the most C\u2010terminal 20,000 daltons of the EGF receptor, which contains the three major autophosphoryation sites. Despite the loss of these sites the EGF receptor from CHO 11 cells binds EGF, demonstrates protein tyrosine kinase activity in response to EGF, and transduces a mitogenic signal. The CHO 11 receptor protein is still autophosphorylated on alternative tyrosine residues. We conclude that phosphorylation of the three tyrosines (P1, P2, and P3) in the C\u2010terminal domain of the receptor is not required for signal transduction by the EGF receptor in these cells.<\/jats:p>","DOI":"10.1002\/jcp.1041340313","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T11:26:57Z","timestamp":1109417217000},"page":"421-428","source":"Crossref","is-referenced-by-count":12,"title":["Loss of three major auto phosphorylation sites in the EGF receptor does not block the mitogenic action of EGF"],"prefix":"10.1002","volume":"134","author":[{"given":"Stella","family":"Clark","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dorothy J.","family":"Cheng","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J. 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