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Carma1, a CARD‐containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF‐κB activation 1
Author(s) -
Gaide Olivier,
Marti Fabio,
Micheau Olivier,
Bonnet David,
Thome Margot,
Tschopp Jürg
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02414-0
Subject(s) - bcl10 , phosphorylation , microbiology and biotechnology , chemistry , nfkb1 , cancer research , biology , biochemistry , transcription factor , gene
Bcl10, a caspase recruitment domain (CARD)‐containing protein identified from a breakpoint in mucosa‐associated lymphoid tissue (MALT) B lymphomas, is essential for antigen‐receptor‐mediated nuclear factor κB (NF‐κB) activation in lymphocytes. We have identified a novel CARD‐containing protein and interaction partner of Bcl10, named Carma1. Carma1 is predominantly expressed in lymphocytes and represents a new member of the membrane‐associated guanylate kinase family. Carma1 binds Bcl10 via its CARD motif and induces translocation of Bcl10 from the cytoplasm into perinuclear structures. Moreover, expression of Carma1 induces phosphorylation of Bcl10 and activation of the transcription factor NF‐κB. We propose that Carma1 is a crucial component of a novel Bcl10‐dependent signaling pathway in T‐cells that leads to the activation of NF‐κB.