A requirement for CARMA1 in TCR-induced NF-kappa B activation (Q28216751)

2

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Sara M Case

3

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Linda M McAllister-Lucas

4

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Lin Wang

5

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Peter S DiStefano

6

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Gabriel Nuñez

7

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John Bertin

8

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Xin Lin

Signal transduction by lymphocyte antigen receptors

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language of work or name

English

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publication date

September 2002

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published in

Nature Immunology

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volume

3

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issue

9

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page(s)

830-5

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cites work

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Integration of T cell receptor-dependent signaling pathways by adapter proteins

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The role of membrane-associated adaptors in T cell receptor signalling

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Adaptors and molecular scaffolds in immune cell signaling

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The NF-kappa B and I kappa B proteins: new discoveries and insights

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NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses

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Rel/NF-kappa B/I kappa B family: intimate tales of association and dissociation

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Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity

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Costimulatory regulation of T cell function.

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Selective modulation of protein kinase C-theta during T-cell activation

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Protein kinase C-theta participates in NF-kappaB activation induced by CD3-CD28 costimulation through selective activation of IkappaB kinase beta

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PKC-θ is required for TCR-induced NF-κB activation in mature but not immature T lymphocytes

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Antigen-induced translocation of PKC-theta to membrane rafts is required for T cell activation

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CIPER, a novel NF kappaB-activating protein containing a caspase recruitment domain with homology to Herpesvirus-2 protein E10

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CLAP, a novel caspase recruitment domain-containing protein in the tumor necrosis factor receptor pathway, regulates NF-kappaB activation and apoptosis

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Equine herpesvirus-2 E10 gene product, but not its cellular homologue, activates NF-kappaB transcription factor and c-Jun N-terminal kinase

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Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and mutated in multiple tumor types

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mE10, a novel caspase recruitment domain-containing proapoptotic molecule

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Inactivating mutations and overexpression of BCL10, a caspase recruitment domain-containing gene, in MALT lymphoma with t(1;14)(p22;q32)

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Bcl10 is a positive regulator of antigen receptor-induced activation of NF-kappaB and neural tube closure

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CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B

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7 January 2021

CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B

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Carma1, a CARD-containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF-kappaB activation

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Bimp1, a MAGUK family member linking protein kinase C activation to Bcl10-mediated NF-kappaB induction

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Card10 is a novel caspase recruitment domain/membrane-associated guanylate kinase family member that interacts with BCL10 and activates NF-kappa B

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Signaling pathways are focused at specialized regions of the plasma membrane by scaffolding proteins of the MAGUK family

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High-frequency mutagenesis of human cells and characterization of a mutant unresponsive to both alpha and gamma interferons

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Bcl10 and MALT1, independent targets of chromosomal translocation in malt lymphoma, cooperate in a novel NF-kappa B signaling pathway

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Induction of gadd45beta by NF-kappaB downregulates pro-apoptotic JNK signalling.

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Inhibition of JNK activation through NF-kappaB target genes

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