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

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

Proc Natl Acad Sci U S A 2000 Feb 29;97(5):2180-4.

SWAP-70 is a component of an enzyme complex that recombines Ig switch regions in vitro. We report here the cloning of 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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