Identification and characterization of a novel cytoskeleton-associated pp60src substrate

Autor:	Albert B. Reynolds, Hong Wu, S B Kanner, R R Vines, J T Parsons
Rok vydání:	1991
Předmět:	Podosome Tyrosine phosphorylation macromolecular substances Cell Biology Biology Subcellular localization Molecular biology SH3 domain chemistry.chemical_compound chemistry biology.protein Cytoskeleton Molecular Biology Peptide sequence Actin Cortactin
Zdroj:	Molecular and Cellular Biology. 11:5113-5124
ISSN:	1098-5549 0270-7306
DOI:	10.1128/mcb.11.10.5113
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::e65002acb2b8712d7b7df91ea868a747 https://doi.org/10.1128/mcb.11.10.5113 Zobrazit plný text záznamu