BANK1 and BLK Act through Phospholipase C Gamma 2 in B-Cell Signaling

被引：44

作者：

Bernal-Quiros, Manuel ^{[1
]}

Wu, Ying-Yu ^{[2
]}

Alarcon-Riquelme, Marta E. ^{[1
,2
]}

Castillejo-Lopez, Casimiro ^{[1
]}

机构：

[1] Pfizer Univ Granada Junta de Andalucia, Ctr Genom & Invest Oncol, Granada, Spain

[2] Oklahoma Med Res Fdn, Arthrit & Clin Immunol Program, Oklahoma City, OK 73104 USA

来源：

PLOS ONE | 2013年 / 8卷 / 03期

基金：

瑞典研究理事会; 美国国家卫生研究院;

关键词：

TYROSINE KINASES; SCAVENGER RECEPTOR; SOLUBLE CD163; CUTTING EDGE; C-GAMMA-2; LYN; SRC; PHOSPHORYLATION; ACTIVATION; PROTEIN;

D O I：

10.1371/journal.pone.0059842

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The B cell adaptor protein with ankyrin repeats (BANK1) and the B lymphoid tyrosine kinase (BLK) have been genetically associated with autoimmunity. The proteins of these genes interact physically and work in concert during B-cell signaling. Little is know about their interactions with other B-cell signaling molecules or their role in the process. Using yeast two hybrid (Y2H) we sought for factors that interact with BANK1. We found that the molecular switch PLCg2 interacts with BANK1 and that the interaction is promoted by B-cell receptor (BCR) stimulation. We found further that the kinase activity of BLK enhanced BANK1-PLCg2 binding and that the interaction was suppressed upon BLK depletion. Immunoprecipitation and mutational analysis demonstrated that the interaction between BANK1 and PLCg2 was dependent on specific tyrosine and proline residues on the adaptor protein. Our results provide new information important to understand the role of these two genes in basic B-cell physiology and immune-related diseases.

引用

页数：12

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