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.

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 …

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 …

Following B-cell antigen receptor (BCR) ligation, the cytoplasmic domains of immunoglobulin α (Igα) and Igβ recruit Syk to initiate signaling cascades. The coupling of Syk to several distal substrates requires linker protein BLNK. However, the ...

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.

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.

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.

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.

Oct 16, 2024 · Here, we elucidate that C-type lectin receptors (CLRs) govern the Syk-mediated activation of BLNK, leading to the inhibition of macrophage migration by disrupting podosome ring formation upon stimulation with fungal β-glucans or α-mannans.

Dec 3, 1999 · In B cells, B cell linker protein (BLNK) links the B cell receptor (BCR)–activated Syk kinase to the phosphoinositide and mitogen-activated kinase pathways. To examine the in vivo role of BLNK, mice deficient in BLNK were generated.