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Association of SWAP-70 with the B cell antigen receptor complex.


ABSTRACT: 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.

SUBMITTER: Masat L 

PROVIDER: S-EPMC15774 | biostudies-literature | 2000 Feb

REPOSITORIES: biostudies-literature

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Association of SWAP-70 with the B cell antigen receptor complex.

Masat L L   Caldwell J J   Armstrong R R   Khoshnevisan H H   Jessberger R R   Herndier B B   Wabl M M   Ferrick D D  

Proceedings of the National Academy of Sciences of the United States of America 20000201 5


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 fu  ...[more]

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