Association of SWAP-70 with the B Cell Antigen Receptor Complex

SWAP-70 is a component of an enzyme complex that recombines Ig switch regions in vitro. We report here the cloning of the human cDNA and its B lymphocyte-specific expression. Although its sequence contains three nuclear localization signals, in small resting B cells, SWAP-70 is mainly found in the c...

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Published in:Proceedings of the National Academy of Sciences - PNAS Vol. 97; no. 5; pp. 2180 - 2184
Main Authors: Masat, L., Caldwell, J., Armstrong, R., Khoshnevisan, H., Jessberger, R., Herndier, B., Wabl, M., Ferrick, D.
Format: Journal Article
Language:English
Published: United States National Academy of Sciences of the United States of America 29-02-2000
National Acad Sciences
National Academy of Sciences
The National Academy of Sciences
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Summary:SWAP-70 is a component of an enzyme complex that recombines Ig switch regions in vitro. We report here the cloning of the human cDNA and its B lymphocyte-specific expression. Although its sequence contains three nuclear localization signals, in small resting B cells, SWAP-70 is mainly found in the cytoplasm. On stimulation, SWAP-70 translocates to the nucleus. In activated, class-switching B cell cultures, it is associated with membrane IgG, but not IgM. The membrane Ig association requires a functional pleckstrin homology domain and is controlled by the C terminus. We suggest that SWAP-70 is involved not only in nuclear events but also in signaling in B cell activation.
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To whom reprint requests should be addressed. E-mail: mutator@itsa.ucsf.edu.
Edited by Gerald R. Crabtree, Stanford University School of Medicine, Stanford, CA, and approved December 27, 1999
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.040374497