Feb 2, 2001 · The SH2 domain-dependent interaction of Btk with BLNK may induce a conformational change in Btk that enables it to serve as the Syk substrate, or alternatively may prompt the appropriate colocalization of Btk and Syk …

BLNK’s function and interaction shown in a schematic of BCR signaling pathways. BCR antigen recognition activates Src family kinases, including the SYK and BTK tyrosine kinases. Syk then phosphorylates BLNK, which can recruit downstream signaling molecules such …

Jul 1, 1998 · We report here the identification and characterization of a novel PTK substrate, BLNK, which is phosphorylated by Syk. Overexpression of wild-type BLNK results in enhanced tyrosine phosphorylation of PLCγ, receptor-mediated calcium responses and transcriptional activation of NF-AT.

Jan 1, 1999 · BLNK (B cell LiNKer protein), a substrate for Syk, is now shown to be essential in activating phospholipase C (PLC)γ2 and JNK. The BCR-induced PLCγ2 activation, but not the JNK activation, was restored by introduction of PLCγ2 membrane-associated form into BLNK-deficient B cells.

This review presents a general introduction to Syk as a signaling molecule, discusses the role of Syk in macrophage-mediated inflammatory responses, and summarizes Syk-related inflammatory diseases and Syk inhibitors that could be candidates for the treatment of these diseases.

We describe here the identification of a novel B cell linker protein, termed BLNK, that interfaces the B cell receptor-associated Syk tyrosine kinase with PLCgamma, the Vav guanine nucleotide exchange factor, and the Grb2 and Nck adapter proteins.

Feb 1, 2009 · Downstream of Syk, B cell linker protein (BLNK) and phospholipase Cγ2 (PLCγ2) also show lower phosphorylation levels upon BTLA signaling, indicating reduced activity of the BCR signal transduction cascade.

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.

Syk/BLNK/NF-κB signaling promotes pancreatic injury induced by tacrolimus and rapamycin has a potentially protective effect by down-regulating NF-κB. Further validation and clinical studies are needed in the future.

Jan 1, 2000 · Recent identification of BLNK as one of the major Btk SH2 binding proteins (Hashimoto et al. 1999; Su et al. 1999) has inspired the novel idea that BLNK, phosphorylated by Syk, provides docking sites for Btk as well as PLC-γ2, …