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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.

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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 , Sylvia Trouliaris , Gerd Helftenbein , Heiner Niemann ^¶ and Teruko Tamura

From the  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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