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Details on Person Phosphorylation of CARMA1 causes conformational change such ...
| Class:Id | Summation:2685549 |
|---|---|
| _displayName | Phosphorylation of CARMA1 causes conformational change such ... |
| _timestamp | 2013-01-23 05:01:28 |
| created | [InstanceEdit:2685567] Garapati, P V, 2012-12-03 |
| literatureReference | [LiteratureReference:2685482] Antigen receptor signaling to NF-kappaB via CARMA1, BCL10, and MALT1 [LiteratureReference:203256] The roles of CARMA1, Bcl10, and MALT1 in antigen receptor signaling [LiteratureReference:2685164] MALT1/paracaspase is a signaling component downstream of CARMA1 and mediates T cell receptor-induced NF-kappaB activation [LiteratureReference:2685296] The Bcl10-Malt1 complex segregates Fc epsilon RI-mediated nuclear factor kappa B activation and cytokine production from mast cell degranulation |
| modified | [InstanceEdit:2997495] Garapati, P V, 2013-01-23 |
| text | 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. |
| (summation) | [Reaction:2730836] Interaction of BCL10:MALT1 with CARMA1 to form CBM complex [Homo sapiens] [Reaction:2730893] Interaction of Bcl10:Malt1 with Carma1 to form CBM complex [Mus musculus] |
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