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. 1991 Oct;11(10):5113–5124. doi: 10.1128/mcb.11.10.5113

Identification and characterization of a novel cytoskeleton-associated pp60src substrate.

H Wu 1, A B Reynolds 1, S B Kanner 1, R R Vines 1, J T Parsons 1
PMCID: PMC361526  PMID: 1922035

Abstract

Transformation of cells by the src oncogene results in elevated tyrosine phosphorylation of two related proteins, p80 and p85 (p80/85). Immunostaining with specific monoclonal antibodies revealed a striking change of subcellular localization of p80/85 in src-transformed cells. p80/85 colocalizes with F-actin in peripheral extensions of normal cells and rosettes (podosomes) of src-transformed cells. Sequence analysis of cDNA clones encoding p80/85 revealed an amino-terminal domain composed of six copies of a direct tandem repeat, each repeat containing 37 amino acids, a carboxyl-terminal SH3 domain, and an interdomain region composed of a highly charged acidic region and a region rich in proline, serine, and threonine. The multidomain structure of p80/85 and its colocalization with F-actin in normal and src-transformed cells suggest that these proteins may associate with components of the cytoskeleton and contribute to organization of cell structure.

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Selected References

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