Interaction of Bcl10:Malt1 with Carma1 to form CBM complex

Stable Identifier
R-MMU-2730893
Type
Reaction [binding]
Species
Mus musculus
Compartment
ReviewStatus
5/5
General
SVG |   | PPTX  | SBGN
Interaction of Bcl10:Malt1 with Carma1 to form CBM complex
Phosphorylation of CARMA1 causes conformational change such that its CARD motif is exposed and is free to interact with BCL10 CARD motif. BCL10 constitutively associated with MALT1 and exists as a preformed complex in the cytoplasm. BCL10 and MALT1 have been identified as key positive regulators of FCERI-dependent NF-kB activation (Klemm et al. 2006). The resulting CARMA1-BCL10-MALT1 (CBM) complex may be stabilized by interactions between the CARMA1 coiled coil (CC) domain and a C-terminal MALT1 region that lacks the DD and first two Ig domains (Thome et al. 2010, Che et al. 2004). The CBM complex transmits activating signals that ultimately result in ubiquitination (Ub) and degradation of the NF-kB inhibitor, IkBa.
Literature References
PubMed ID Title Journal Year
16432253 The Bcl10-Malt1 complex segregates Fc epsilon RI-mediated nuclear factor kappa B activation and cytokine production from mast cell degranulation

Klemm, S, Gutermuth, J, Hültner, L, Sparwasser, T, Behrendt, H, Peschel, C, Mak, TW, Jakob, T, Ruland, J

J. Exp. Med. 2006
11262391 Bcl10 and MALT1, independent targets of chromosomal translocation in malt lymphoma, cooperate in a novel NF-kappa B signaling pathway

Lucas, PC, Yonezumi, M, Inohara, N, McAllister-Lucas, LM, Abazeed, ME, Chen, FF, Yamaoka, S, Seto, M, Nunez, G

J. Biol. Chem. 2001
14754896 MALT1/paracaspase is a signaling component downstream of CARMA1 and mediates T cell receptor-induced NF-kappaB activation

Che, T, You, Y, Wang, D, Tanner, MJ, Dixit, VM, Lin, X

J. Biol. Chem. 2004
22880103 Structural insights into the assembly of CARMA1 and BCL10

Li, S, Yang, X, Shao, J, Shen, Y

PLoS ONE 2012
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Orthologous Events
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