Cbl-b positively regulates Btk-mediated activation of phospholipase C-gamma2 in B cells.
Cbl-b positively regulates Btk-mediated activation of phospholipase C-gamma2 in B cells.
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DOI：
10.1084/jem.20020068
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发表时间：
2002-07-01
期刊：
影响因子：
--
通讯作者：
Yamamoto T
中科院分区：
文献类型：
--
作者：
Yasuda T;Tezuka T;Maeda A;Inazu T;Yamanashi Y;Gu H;Kurosaki T;Yamamoto T
Genetic studies have revealed that Cbl-b plays a negative role in the antigen receptor–mediated proliferation of lymphocytes. However, we show that Cbl-b–deficient DT40 B cells display reduced phospholipase C (PLC)-γ2 activation and Ca2+ mobilization upon B cell receptor (BCR) stimulation. In addition, the overexpression of Cbl-b in WEHI-231 mouse B cells resulted in the augmentation of BCR-induced Ca2+ mobilization. Cbl-b interacted with PLC-γ2 and helped the association of PLC-γ2 with Bruton's tyrosine kinase (Btk), as well as B cell linker protein (BLNK). Cbl-b was indispensable for Btk-dependent sustained increase in intracellular Ca2+. Both NH2-terminal tyrosine kinase-binding domain and COOH-terminal half region of Cbl-b were essential for its association with PLC-γ2 and the regulation of Ca2+ mobilization. These results demonstrate that Cbl-b positively regulates BCR-mediated Ca2+ signaling, most likely by influencing the Btk/BLNK/PLC-γ2 complex formation.
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影响因子：
4.8
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影响因子：
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DOI：
10.1084/jem.188.7.1287
发表时间：
1998-10-05
期刊：
The Journal of experimental medicine
影响因子：
--
作者：
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通讯作者：
Kurosaki T