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 |
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Main Authors: | , , , , , , , |
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 |
Subjects: | |
Online Access: | Get full text |
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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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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 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 |