c-Src association with and phosphorylation of p58gag, a membrane- and microfilament-associated retroviral Gag-like protein in a xenotransplantable rat mammary tumor View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1999-07-15

AUTHORS

Jiaqi Huang, Bao-Tong Zhang, Yongqing Li, Bruce Mayer, Kermit L Carraway, Coralie A Carothers Carraway

ABSTRACT

The retroviral Gag-like protein p58gag expressed in a highly metastatic ascites rat mammary adenocarcinoma has been implicated in cell surface changes contributing to xenotransplantability. p58gag is present in the cells in a plasma membrane- and microfilament-associated signal transduction particle containing Src and is phosphorylated on tyrosine. Overlay analyses and affinity chromatography with glutathione S-transferase (GST) fusion proteins of Src homology-3 (SH3) domains showed direct binding of the Src but not the Crk SH3 domain to p58gag. This association was confirmed by co-immunoprecipitation of partially purified p58gag from ascites cell lysates with platelet Src. Further, a GST-p58gag fusion protein bound full length c-Src from either platelets or c-Src-expressing insect cells. The GST-p58gag fusion protein, but not GST, was phosphorylated by platelet or insect cell-expressed c-Src, but not by a kinase negative c-Src variant. The binding of GST-p58gag to c-Src was almost completely abolished by a 50-fold excess of the GST-SH3 domain of Src, and a parallel decrease in tyrosine phosphorylation of p58gag was observed. These results demonstrate that p58gag is tyrosine-phosphorylated as a consequence of its specific association with c-Src via its SH3 domain. These observations suggest a mechanism by which Gag proteins may contribute to retroviral maturation or pathogenesis through binding and relocalization of SH3 domain-containing proteins such as Src-like tyrosine kinases to sites of association of microfilaments with the plasma membrane. More... »

PAGES

4099-4107

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/sj.onc.1202779

DOI

http://dx.doi.org/10.1038/sj.onc.1202779

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1053007338

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10435591


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