Phosphorylation of rap1GAP in vivo and by cAMP-dependent kinase and the cell cycle p34cdc2 kinase in vitro.
作者： P Polakis , B Rubinfeld , F McCormick
DOI: 10.1016/S0021-9258(19)50086-2
关键词:
摘要: rap1GAP is a GTPase activating protein that specifically stimulates the GTP hydrolytic rate of ras-related p21rap1.rap1GAP undergoes post-translational modification causes substantial change in its mobility on sodium dodecyl sulfate-polyacrylamide gels. At least part this due to phosphorylation. Expression cDNA insect cells labeled with 32Pi resulted high level incorporation radioactivity into serine residues expressed protein. Purified was phosphorylated vitro by cAMP-dependent kinase and cell cycle p34cdc2 kinase. The molar ratio incorporated phosphate/rap1GAP approximately 3 2 p34cdc2. sites phosphorylation both kinases were localized 100-residue segment contained carboxyl-terminal region predicted primary structure rap1GAP. Highly favorable recognition sequences for two are within fragment proposed as Treatment SK-MEL-3 dibutyryl cAMP promoted vivo. Based results comparative phosphopeptide mapping vivo identical.
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