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Novel autophosphorylation sites of Src family kinases regulate kinase activity and SH2 domain-binding capacity.
Weir, Marion E; Mann, Jacqueline E; Corwin, Thomas; Fulton, Zachary W; Hao, Jennifer M; Maniscalco, Jeanine F; Kenney, Marie C; Roman Roque, Kristal M; Chapdelaine, Elizabeth F; Stelzl, Ulrich; Deming, Paula B; Ballif, Bryan A; Hinkle, Karen L.
Afiliación
  • Weir ME; Department of Biology, University of Vermont, Burlington, VT, USA.
  • Mann JE; Department of Medical Laboratory and Radiation Sciences, University of Vermont, Burlington, VT, USA.
  • Corwin T; Otto-Warburg Laboratory, Max Planck Institute for Molecular Genetics, Berlin, Germany.
  • Fulton ZW; Department of Biology, University of Vermont, Burlington, VT, USA.
  • Hao JM; Department of Biology and Physical Education, Norwich University, Northfield, VT, USA.
  • Maniscalco JF; Department of Biology, University of Vermont, Burlington, VT, USA.
  • Kenney MC; Department of Biology, University of Vermont, Burlington, VT, USA.
  • Roman Roque KM; Department of Biology, University of Vermont, Burlington, VT, USA.
  • Chapdelaine EF; Department of Biology, University of Vermont, Burlington, VT, USA.
  • Stelzl U; Department of Biology, University of Vermont, Burlington, VT, USA.
  • Deming PB; Department of Biology and Physical Education, Norwich University, Northfield, VT, USA.
  • Ballif BA; Otto-Warburg Laboratory, Max Planck Institute for Molecular Genetics, Berlin, Germany.
  • Hinkle KL; Department of Medical Laboratory and Radiation Sciences, University of Vermont, Burlington, VT, USA.
FEBS Lett ; 590(8): 1042-52, 2016 04.
Article en En | MEDLINE | ID: mdl-27001024
Src family tyrosine kinases (SFKs) are critical players in normal and aberrant biological processes. While phosphorylation importantly regulates SFKs at two known tyrosines, large-scale phosphoproteomics have revealed four additional tyrosines commonly phosphorylated in SFKs. We found these novel tyrosines to be autophosphorylation sites. Mimicking phosphorylation at the C-terminal site to the activation loop decreased Fyn activity. Phosphomimetics and direct phosphorylation at the three SH2 domain sites increased Fyn activity while reducing phosphotyrosine-dependent interactions. While 68% of human SH2 domains exhibit conservation of at least one of these tyrosines, few have been found phosphorylated except when found in cis to a kinase domain.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Familia-src Quinasas / Dominios Homologos src Límite: Humans Idioma: En Revista: FEBS Lett Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
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XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Familia-src Quinasas / Dominios Homologos src Límite: Humans Idioma: En Revista: FEBS Lett Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido