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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Cell Transformation, Viral
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In Vitro Techniques
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Moloney murine sarcoma virus / genetics
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Mutation
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Oncogene Proteins v-mos
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Phosphorylation
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Protein Kinases / genetics*
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Protein Kinases / metabolism
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Protein Serine-Threonine Kinases
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Retroviridae Proteins / genetics*
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Retroviridae Proteins / metabolism
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Transformation, Genetic
Substances
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Oncogene Proteins v-mos
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Retroviridae Proteins
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Protein Kinases
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Protein Serine-Threonine Kinases