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

Wu H, Reynolds AB, Kanner SB, Vines RR, Parsons JT
Mol Cell Biol. 1991 11 (10): 5113-24

PMID: 1922035 · PMCID: PMC361526 · DOI:10.1128/mcb.11.10.5113

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.

MeSH Terms (21)

Amino Acid Sequence Animals Avian Proteins Base Sequence Blotting, Northern Blotting, Western Cells, Cultured Cell Transformation, Viral Chick Embryo Cloning, Molecular Cytoskeletal Proteins Cytoskeleton Microscopy, Fluorescence Molecular Sequence Data Oncogene Protein pp60(v-src) Phosphorylation Protein Conformation Repetitive Sequences, Nucleic Acid Serine Threonine Tyrosine

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