Related Experiment Videos
Transforming mutant v-mos protein kinases that are deficient in in vitro autophosphorylation
1Department of Chemistry, University of California, San Diego, La Jolla 92093.
Molecular and Cellular Biology
|September 1, 1989
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.