Abstract:
:Protein kinase C (PKC) and Syk protein tyrosine kinase play critical roles in immune cell activation including that through the high-affinity IgE receptor, FcepsilonRI. Mechanisms by which PKC activation leads to the activation of Ras, a family of GTPases essential for immune cell activation, have been elusive. We present evidence that Tyr-662 and Tyr-658 of PKCbetaI and PKCalpha, respectively, are phosphorylated by Syk in the membrane compartment of FcepsilonRI-stimulated mast cells. These phosphorylations require prior PKC autophosphorylation of the adjacent serine residues (Ser-661 and Ser-657, respectively) and generate a binding site for the SH2 domain of the adaptor protein Grb-2. By recruiting the Grb-2/Sos complex to the plasma membrane, these conventional PKC isoforms contribute to the full activation of the Ras/extracellular signal-regulated kinase signaling pathway in FcepsilonRI-stimulated mast cells.
journal_name
Proc Natl Acad Sci U S Aauthors
Kawakami Y,Kitaura J,Yao L,McHenry RW,Kawakami Y,Newton AC,Kang S,Kato RM,Leitges M,Rawlings DJ,Kawakami Tdoi
10.1073/pnas.1633695100keywords:
subject
Has Abstractpub_date
2003-08-05 00:00:00pages
9470-5issue
16eissn
0027-8424issn
1091-6490pii
1633695100journal_volume
100pub_type
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