title: Transforming mutant v-mos protein kinases that are deficient in in vitro autophosphorylation.
abstract: We investigated the importance of specific serine residues for autophosphorylation and transformation by serine-threonine protein kinase p37mos. When either serine 326 or 358 was replaced with alanine, the resulting mutant protein retained the ability to transform NIH 3T3 cells but failed to autophosphorylate in vitro. These studies represent the first functional uncoupling of these two activities for p37mos.
authors.affiliation: Department of Chemistry, University of California, San Diego, La Jolla 92093.
authors.forename: R S
authors.initials: RS
authors.lastname: Freeman
authors.forename: D J
authors.initials: DJ
authors.lastname: Donoghue
mesh_terms: D000818:Animals; D002472:Cell Transformation, Viral; D066298:In Vitro Techniques; D008980:Moloney murine sarcoma virus / Q000235:genetics; D009154:Mutation; D017232:Oncogene Proteins v-mos; D010766:Phosphorylation; D011494:Protein Kinases / Q000235:genetics* / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases; D012191:Retroviridae Proteins / Q000235:genetics* / Q000378:metabolism; D014170:Transformation, Genetic
chemical_list: D017232:Oncogene Proteins v-mos; D012191:Retroviridae Proteins; D011494:Protein Kinases; D017346:Protein Serine-Threonine Kinases