High impact information on BRDG1

• BRDG1 thus appears to function as a docking protein acting downstream of Tec in BCR signaling [1].
• Efficient phosphorylation of BRDG1 by Tec required the PH and SH2 domains as well as the kinase domain of the latter [1].
• BRDG1 contains a proline-rich motif, a PH domain, and multiple tyrosine residues that are potential target sites for Src homology 2 domains [1].
• BRDG1 transcripts are abundant in the human B cell line Ramos, and the endogenous protein underwent tyrosine phosphorylation in response to BCR stimulation [1].
• We cloned a novel adaptor molecule, signal transducing adaptor protein (STAP)-2 containing PH and SH2-like domains as a c-fms interacting protein [2].

Biological context of BRDG1

• Three isoforms of BRDG1 are generated by alternative splicing of the message [3].
• The deubiquitinase AMSH (associated molecule with the SH3 domain of signal transducing adaptor molecule) specifically interacts with phosphorylated Xp95 in M-phase cell lysates [4].

Other interactions of BRDG1

• TRAF2 is a signal transducing adaptor molecule which binds to the CD40 cytoplasmic domain [5].

Analytical, diagnostic and therapeutic context of BRDG1

• Molecular cloning of a docking protein, BRDG1, that acts downstream of the Tec tyrosine kinase [1].
• Before introduction of the proforma, junior medical staff were instructed in the procedure using specialised lumbar puncture manikins (Baby Stap; Laerdel, USA) [6].

References