Identification of phosphorylation sites within the SH3 domains of Tec family tyrosine kinases (Q28207891)

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Pekka T Mattsson

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Per Antonsson

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Anna Westlund

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Johan Lennartsson

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Henrik Hansson

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Peter Löw

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Lars Rönnstrand

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C I Edvard Smith

Biochimica et Biophysica Acta

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language of work or name

English

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publication date

21 February 2003

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published in

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volume

1645

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issue

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page(s)

123-32

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cites work

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Tec kinases: a family with multiple roles in immunity

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Tec kinases: modulators of lymphocyte signaling and development

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The gene involved in X-linked agammaglobulinaemia is a member of the src family of protein-tyrosine kinases

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Colocalization of X-linked agammaglobulinemia and X-linked immunodeficiency genes

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Mutation of unique region of Bruton's tyrosine kinase in immunodeficient XID mice

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T cell receptor-initiated calcium release is uncoupled from capacitative calcium entry in Itk-deficient T cells

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Altered T cell receptor signaling and disrupted T cell development in mice lacking Itk.

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Src family tyrosine kinases and growth factor signaling

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Structure-function relationships in Src family and related protein tyrosine kinases

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Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases

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Tec protein-tyrosine kinase is an effector molecule of Lyn protein-tyrosine kinase

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Lck phosphorylates the activation loop tyrosine of the Itk kinase domain and activates Itk kinase activity

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Regulation of Btk function by a major autophosphorylation site within the SH3 domain

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Solution structure of the SH3 domain from Bruton's tyrosine kinase

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Intermolecular interactions between the SH3 domain and the proline-rich TH region of Bruton's tyrosine kinase.

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Both proline-rich sequences in the TH region of Bruton's tyrosine kinase stabilize intermolecular interactions with the SH3 domain.

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Competing modes of self-association in the regulatory domains of Bruton's tyrosine kinase: Intramolecular contact versus asymmetric homodimerization

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Proline-rich sequences that bind to Src homology 3 domains with individual specificities

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Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain

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Requirement for Tec kinases Rlk and Itk in T cell receptor signaling and immunity

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The SH3 domain of Bruton's tyrosine kinase displays altered ligand binding properties when auto-phosphorylated in vitro

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Novel recognition mode between Vav and Grb2 SH3 domains

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Requirement for c-Src catalytic activity and the SH3 domain in platelet-derived growth factor BB and epidermal growth factor mitogenic signaling

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The PDGF receptor phosphorylates Tyr 138 in the c-Src SH3 domain in vivo reducing peptide ligand binding

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