Complexes of gamma-tubulin with nonreceptor protein tyrosine kinases Src and Fyn in differentiating P19 embryonal carcinoma cells
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
15242776
DOI
10.1016/j.yexcr.2004.04.016
PII: S0014482704002186
Knihovny.cz E-zdroje
- MeSH
- buněčná diferenciace fyziologie MeSH
- fosforylace MeSH
- fosfotyrosin antagonisté a inhibitory metabolismus MeSH
- inhibitory enzymů farmakologie MeSH
- kmenové buňky embryonálního karcinomu MeSH
- kmenové buňky cytologie metabolismus MeSH
- makromolekulární látky MeSH
- mikrotubuly metabolismus MeSH
- modulátory tubulinu MeSH
- myši MeSH
- nádorové buňky kultivované MeSH
- nádorové kmenové buňky metabolismus patologie MeSH
- neurony cytologie metabolismus MeSH
- protilátky farmakologie MeSH
- protoonkogenní proteiny c-fyn MeSH
- protoonkogenní proteiny antagonisté a inhibitory metabolismus MeSH
- skupina kinas odvozených od src-genu antagonisté a inhibitory metabolismus MeSH
- terciární struktura proteinů genetika MeSH
- tubulin metabolismus MeSH
- upregulace fyziologie MeSH
- vazba proteinů genetika MeSH
- vazebná místa genetika MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- fosfotyrosin MeSH
- Fyn protein, mouse MeSH Prohlížeč
- inhibitory enzymů MeSH
- makromolekulární látky MeSH
- modulátory tubulinu MeSH
- protilátky MeSH
- protoonkogenní proteiny c-fyn MeSH
- protoonkogenní proteiny MeSH
- skupina kinas odvozených od src-genu MeSH
- tubulin MeSH
Nonreceptor protein tyrosine kinases of the Src family have been shown to play an important role in signal transduction as well as in regulation of microtubule protein interactions. Here we show that gamma-tubulin (gamma-Tb) in P19 embryonal carcinoma cells undergoing neuronal differentiation is phosphorylated and forms complexes with protein tyrosine kinases of the Src family, Src and Fyn. Elevated expression of both kinases during differentiation corresponded with increased level of proteins phosphorylated on tyrosine. Immunoprecipitation experiments with antibodies against Src, Fyn, gamma-tubulin, and with anti-phosphotyrosine antibody revealed that gamma-tubulin appeared in complexes with these kinases. In vitro kinase assays showed tyrosine phosphorylation of proteins in gamma-tubulin complexes isolated from differentiated cells. Pretreatment of cells with Src family selective tyrosine kinase inhibitor PP2 reduced the amount of phosphorylated gamma-tubulin in the complexes. Binding experiments with recombinant SH2 and SH3 domains of Src and Fyn kinases revealed that protein complexes containing gamma-tubulin bound to SH2 domains and that these interactions were of SH2-phosphotyrosine type. The combined data suggest that Src family kinases might have an important role in the regulation of gamma-tubulin interaction with tubulin dimers or other proteins during neurogenesis.
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