PI3Ks (phosphoinositide 3-kinases) play critical roles in BCR (B-cell receptor) signalling via the generation of 3-phosphoinositide second messengers. Recruitment of PH domain (pleckstrin homology domain)-containing signal transduction proteins to the plasma membrane through binding to 3-phosphoinositide second messengers represents a major effector mechanism for PI3Ks. Here, we review data on the PH domain-containing adaptor protein Bam32 (B-cell adaptor molecule of 32 kDa)/DAPP1 (dual adaptor for phosphotyrosine and 3-phosphoinositides 1), focusing on its functions in B-lymphocyte activation. Present results support the view that Bam32/DAPP1 mediates multiple PI3K-dependent responses in B-cells through membrane-proximal mechanisms involving Src kinases, Rac1, F-actin and mitogen-activated protein kinases, resulting in selective effects on BCR-mediated proliferation, antigen presentation and generation of antibody responses.
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April 2007
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Conference Article|
March 20 2007
Regulation of B-lymphocyte activation by the PH domain adaptor protein Bam32/DAPP1
A.J. Marshall;
A.J. Marshall
1
1Department of Immunology, University of Manitoba, 730 William Avenue, Winnipeg, MB, Canada, R3E 0W3
1To whom correspondence should be addressed (email marshall@ms.umanitoba.ca).
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T. Zhang;
T. Zhang
1Department of Immunology, University of Manitoba, 730 William Avenue, Winnipeg, MB, Canada, R3E 0W3
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M. Al-Alwan
M. Al-Alwan
1Department of Immunology, University of Manitoba, 730 William Avenue, Winnipeg, MB, Canada, R3E 0W3
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Biochem Soc Trans (2007) 35 (2): 181–182.
Article history
Received:
November 30 2006
Citation
A.J. Marshall, T. Zhang, M. Al-Alwan; Regulation of B-lymphocyte activation by the PH domain adaptor protein Bam32/DAPP1. Biochem Soc Trans 1 April 2007; 35 (2): 181–182. doi: https://doi.org/10.1042/BST0350181
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