Tyrosine phosphorylation of a mitogen-activated protein kinase-like protein occurs at a late step in exocytosis. Studies with tyrosine phosphatase inhibitors and various secretagogues in rat RBL-2H3 cells.

This publication has 43 references indexed in Scilit:

• Signal transduction by Fc receptors: the Fc&RI case
  Immunology Today, 1993
• The MAP kinase cascade is essential for diverse signal transduction pathways
  Trends in Biochemical Sciences, 1993
• Protein-tyrosine phosphorylation: an essential component of FcεRI signaling
  Immunology Today, 1992
• Inhibition of protein tyrosine phosphatase activity by diamide is reversed by epidermal growth factor in fibroblasts
  FEBS Letters, 1991
• Carbachol induces secretion in a mast cell line (RBL‐2H3) transfected with the ml muscarinic receptor gene
  FEBS Letters, 1991
• Regulation of the antigen-induced F-actin response in rat basophilic leukemia cells by protein kinase C.
  The Journal of cell biology, 1991
• A 42-kD tyrosine kinase substrate linked to chromaffin cell secretion exhibits an associated MAP kinase activity and is highly related to a 42-kD mitogen-stimulated protein in fibroblasts.
  The Journal of cell biology, 1990
• Receptor-mediated release of inositol 1,4,5-trisphosphate and inositol 1,4-bisphosphate in rat basophilic leukemia RBL-2H3 cells permeabilized with streptolysin O
  Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1989
• Two G-proteins act in series to control stimulus-secretion coupling in mast cells: use of neomycin to distinguish between G-proteins controlling polyphosphoinositide phosphodiesterase and exocytosis.
  The Journal of cell biology, 1987
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970