Protein-tyrosine phosphorylation: an essential component of Fc epsilon RI signaling.
Mast cell and basophil activation can be achieved by antigen-mediated aggregation of cell surface Fc epsilon RI molecules. At least two signaling pathways are triggered by this activation. Both involve tyrosine phosphorylation. This aspect of Fc epsilon RI signaling is examined here in detail and its position in a complex network of post-binding events assessed.
Benhamou
M
M
Laboratory of Immunology, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892.
Siraganian
R P
RP
D000818:Animals; D000944:Antigens, Differentiation, B-Lymphocyte / Q000378:metabolism*; D001491:Basophils / Q000378:metabolism; D015471:Leukemia, Basophilic, Acute / Q000378:metabolism / Q000473:pathology; D008407:Mast Cells / Q000378:metabolism; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism; D051381:Rats; D011961:Receptors, Fc / Q000378:metabolism*; D017455:Receptors, IgE; D015398:Signal Transduction; D010738:Type C Phospholipases / Q000378:metabolism
D000944:Antigens, Differentiation, B-Lymphocyte; D011506:Proteins; D011961:Receptors, Fc; D017455:Receptors, IgE; D011505:Protein-Tyrosine Kinases; D010749:Phosphoprotein Phosphatases; D010738:Type C Phospholipases