Phosphatidylinositol 3-kinase-dependent translocation of phospholipase Cgamma2 in mouse megakaryocytes is independent of Bruton tyrosine kinase translocation

Blood. 2001 Feb 1;97(3):678-84. doi: 10.1182/blood.v97.3.678.

Abstract

Activation of the collagen receptor glycoprotein VI (GPVI) by a collagen-related peptide (CRP) induces stimulation of platelets and megakaryocytes through the phosphatidylinositol (PI) 3-kinase-dependent pathway leading to activation of Bruton tyrosine kinase (Btk) and phospholipase Cgamma2 (PLCgamma2). Here, we present evidence that both proteins undergo PI 3-kinase-dependent translocation to the plasma membrane on CRP stimulation that is markedly inhibited by wortmannin and LY294002. Translocation of PLCgamma2 but not Btk is also seen in megakaryocytes from X-linked immunodeficiency mice, which have a mutation that reduces the affinity of the pleckstrin homology (PH) domain of Btk for PI 3,4,5-trisphosphate (PI 3,4,5-P3). Activation of PC12 cells by epidermal growth factor (EGF) results in increased PI 3-kinase activity and high PI 3,4,5-P3 levels that trigger translocation of the green fluorescent protein (GFP)-labeled PH of Btk, but not the GFP-labeled PH and tandem Src homology 2 (SH2) domains of PLCgamma2. In contrast to the results with CRP, the G protein-coupled receptor agonist thrombin stimulates PI 3-kinase-independent translocation of Btk but not PLCgamma2. In conclusion, these results demonstrate that in mouse megakaryocytes, CRP leads to PI 3-kinase-dependent translocation of PLCgamma2 and Btk that are independent of one another, whereas thrombin only induces translocation of Btk through a pathway that is independent of PI 3-kinase activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agammaglobulinaemia Tyrosine Kinase
  • Agammaglobulinemia / enzymology
  • Androstadienes / pharmacology
  • Animals
  • Blood Platelets / drug effects
  • Blood Platelets / enzymology
  • Calcium / metabolism
  • Carrier Proteins*
  • Cell Membrane / drug effects
  • Cell Membrane / metabolism
  • Cells, Cultured
  • Enzyme Inhibitors / pharmacology
  • Enzyme Precursors / metabolism
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Isoenzymes / chemistry
  • Isoenzymes / metabolism*
  • Megakaryocytes / drug effects
  • Megakaryocytes / enzymology*
  • Mice
  • Mice, Mutant Strains
  • Models, Biological
  • Phosphatidylinositol 3-Kinases / physiology*
  • Phosphatidylinositol Phosphates / metabolism
  • Phosphoinositide-3 Kinase Inhibitors
  • Phospholipase C gamma
  • Protein Transport
  • Protein-Tyrosine Kinases / metabolism*
  • Proteins / pharmacology
  • Syk Kinase
  • Thrombin / pharmacology
  • Type C Phospholipases / chemistry
  • Type C Phospholipases / metabolism*
  • Wortmannin
  • X Chromosome
  • src Homology Domains

Substances

  • Androstadienes
  • Carrier Proteins
  • Enzyme Inhibitors
  • Enzyme Precursors
  • Intracellular Signaling Peptides and Proteins
  • Isoenzymes
  • Phosphatidylinositol Phosphates
  • Phosphoinositide-3 Kinase Inhibitors
  • Proteins
  • c1q-binding proteins
  • phosphatidylinositol 3,4,5-triphosphate
  • Protein-Tyrosine Kinases
  • Agammaglobulinaemia Tyrosine Kinase
  • BTK protein, human
  • Btk protein, mouse
  • SYK protein, human
  • Syk Kinase
  • Syk protein, mouse
  • Type C Phospholipases
  • Phospholipase C gamma
  • Thrombin
  • Calcium
  • Wortmannin