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Volume 271, Number 40, Issue of October 4, 1996 pp. 24476-24481
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Tyrosine Phosphorylation of the Juxtamembrane Domain of the v-Fms Oncogene Product Is Required for Its Association with a 55-kDa Protein

(Received for publication, November 27, 1995, and in revised form, May 16, 1996)

Hans Joos Dagger , Sylvia Trouliaris Dagger , Gerd Helftenbein Dagger , Heiner Niemann and Teruko Tamura Dagger

From the Dagger  Institut für Virologie, Justus-Liebig-Universität Giessen, Frankfurter Strasse 107, D-35392 Giessen and the  Institut für Biochemie, OE 4310, Medizinische Hochschule Hannover, D-30625 Hannover, Federal Republic of Germany

Tyrosine autophosphorylation of the v-Fms oncogene product results in the formation of high affinity binding sites for cellular proteins with Src homology 2 (SH2) domains that are involved in various signal cascades. Tryptic digestion of the autophosphorylated v-Fms and of its cellular counterpart, the feline c-Fms polypeptide, gave rise to at least six common major phosphopeptides, four of which have been characterized previously. Employing site-directed mutagenesis and phosphopeptide mapping of in vitro phosphorylated glutathione S-transferase v-Fms fusion proteins as well as full-length v-Fms molecules expressed in various cells, we show here that Tyr543 of the juxtamembrane domain and Tyr696 of the kinase insert domain constitute major autophosphorylation sites. Recombinant fusion proteins containing the tyrosine-phosphorylated kinase insert domain bind the growth factor receptor bound protein 2 and the p85 and p110 subunits of phosphatidylinositol 3'-kinase. In contrast, fusion proteins containing the juxtamembrane domain phosphorylated on Tyr543 fail to bind any of the known SH2 domain-containing cellular proteins but associate specifically with an as yet undefined 55-kDa cellular protein that by itself is phosphorylated on tyrosine.


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