Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins.

Lignende værker

• Distinct p53/56lyn and p59fyn domains associate with nonphosphorylated and phosphorylated Ig-alpha.
  af: Pleiman, C M, et al.
  Udgivet: (1994)
• p56Lck and p59Fyn regulate CD28 binding to phosphatidylinositol 3-kinase, growth factor receptor-bound protein GRB-2, and T cell-specific protein-tyrosine kinase ITK: implications for T-cell costimulation.
  af: Raab, M, et al.
  Udgivet: (1995)
• p56(Lck) anchors CD4 to distinct microdomains on microvilli
  af: Foti, Michelangelo, et al.
  Udgivet: (2002)
• Mapping of sites on the Src family protein tyrosine kinases p55blk, p59fyn, and p56lyn which interact with the effector molecules phospholipase C-gamma 2, microtubule-associated protein kinase, GTPase-activating protein, and phosphatidylinositol 3-kinase.
  af: Pleiman, C M, et al.
  Udgivet: (1993)
• The CD45 tyrosine phosphatase regulates specific pools of antigen receptor-associated p59fyn and CD4-associated p56lck tyrosine in human T-cells.
  af: Biffen, M, et al.
  Udgivet: (1994)