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Immunity ; 10(1): 117-25, 1999 Jan.
Article in English | MEDLINE | ID: mdl-10023776

ABSTRACT

Signaling through the B cell receptor (BCR) is essential for B cell function and development. Despite the key role of Syk in BCR signaling, little is known about the mechanism by which Syk transmits downstream effectors. BLNK (B cell LiNKer protein), a substrate for Syk, is now shown to be essential in activating phospholipase C (PLC)gamma 2 and JNK. The BCR-induced PLC gamma 2 activation, but not the JNK activation, was restored by introduction of PLC gamma 2 membrane-associated form into BLNK-deficient B cells. As JNK activation requires both Rac1 and PLC gamma 2, our results suggest that BLNK regulates the Rac1-JNK pathway, in addition to modulating PLC gamma 2 localization.


Subject(s)
B-Lymphocytes/enzymology , Calcium-Calmodulin-Dependent Protein Kinases/metabolism , Carrier Proteins/physiology , Enzyme Precursors/metabolism , GTP-Binding Proteins/metabolism , Isoenzymes/metabolism , Mitogen-Activated Protein Kinases , Phosphoproteins , Protein-Tyrosine Kinases/metabolism , Type C Phospholipases/metabolism , Adaptor Proteins, Signal Transducing , Amino Acid Sequence , Animals , B-Lymphocytes/metabolism , Calcium Signaling , Carrier Proteins/genetics , Carrier Proteins/metabolism , Cell Membrane/enzymology , Chickens , Enzyme Activation , Humans , Intracellular Signaling Peptides and Proteins , Isoenzymes/biosynthesis , Isoenzymes/genetics , JNK Mitogen-Activated Protein Kinases , Mice , Molecular Sequence Data , Phospholipase C gamma , Phosphorylation , Receptors, Antigen, B-Cell/metabolism , Receptors, Antigen, B-Cell/physiology , Recombinant Fusion Proteins/biosynthesis , Syk Kinase , Type C Phospholipases/biosynthesis , Type C Phospholipases/genetics , Tyrosine/metabolism , rac GTP-Binding Proteins , ras Proteins/metabolism
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