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  1. Article ; Online: CARMA1-mediated NF-kappaB and JNK activation in lymphocytes.

    Blonska, Marzenna / Lin, Xin

    Immunological reviews

    2009  Volume 228, Issue 1, Page(s) 199–211

    Abstract: ... mediate NF-kappaB and JNK activation. In this review, we summarize our findings in revealing the roles ... Activation of transcription factor nuclear factor-kappaB (NF-kappaB) and Jun N-terminal kinase (JNK ... of CARMA1 in the NF-kappaB and JNK signaling pathways in the context of recent advances in this field. ...

    Abstract Activation of transcription factor nuclear factor-kappaB (NF-kappaB) and Jun N-terminal kinase (JNK) play the pivotal roles in regulation of lymphocyte activation and proliferation. Deregulation of these signaling pathways leads to inappropriate immune response and contributes to the development of leukemia/lymphoma. The scaffold protein CARMA1 [caspase-recruitment domain (CARD) membrane-associated guanylate kinase (MAGUK) protein 1] has a central role in regulation of NF-kappaB and the JNK2/c-Jun complex in both B and T lymphocytes. During last several years, tremendous work has been done to reveal the mechanism by which CARMA1 and its signaling partners, B cell CLL-lymphoma 10 and mucosa-associated lymphoid tissue 1, are activated and mediate NF-kappaB and JNK activation. In this review, we summarize our findings in revealing the roles of CARMA1 in the NF-kappaB and JNK signaling pathways in the context of recent advances in this field.
    MeSH term(s) Animals ; CARD Signaling Adaptor Proteins/metabolism ; Humans ; Lymphocyte Activation ; MAP Kinase Kinase 4/metabolism ; NF-kappa B/metabolism ; Signal Transduction
    Chemical Substances CARD Signaling Adaptor Proteins ; NF-kappa B ; MAP Kinase Kinase 4 (EC 2.7.12.2)
    Language English
    Publishing date 2009-03-12
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 391796-4
    ISSN 1600-065X ; 0105-2896
    ISSN (online) 1600-065X
    ISSN 0105-2896
    DOI 10.1111/j.1600-065X.2008.00749.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Serine 649 phosphorylation within the protein kinase C-regulated domain down-regulates CARMA1 activity in lymphocytes.

    Moreno-García, Miguel E / Sommer, Karen / Haftmann, Claudia / Sontheimer, Clayton / Andrews, Sarah F / Rawlings, David J

    Journal of immunology (Baltimore, Md. : 1950)

    2009  Volume 183, Issue 11, Page(s) 7362–7370

    Abstract: Phosphorylation of CARMA1 is a crucial event initiating the assembly of IkappaB kinase and JNK ... S657) resulted in reduced NF-kappaB activation, whereas mutation of the third serine (S649) had no ... loss of S649 (by mutation to alanine) promotes enhanced IkappaB kinase and JNK activation in both B and ...

    Abstract Phosphorylation of CARMA1 is a crucial event initiating the assembly of IkappaB kinase and JNK signaling complexes downstream of activated Ag receptors. We previously mapped three protein kinase C (PKC) target sites in murine CARMA1 in vitro, and demonstrated that mutation of two of these serines (S564 and S657) resulted in reduced NF-kappaB activation, whereas mutation of the third serine (S649) had no clear effect. In this study, we report that when low concentrations of Ag receptor activators are used, loss of S649 (by mutation to alanine) promotes enhanced IkappaB kinase and JNK activation in both B and T cell lines. Reconstitution of CARMA1(-/-) DT40 B cells with CARMA1 S649A leads to increased cell death and reduced cell growth in comparison to wild-type CARMA1, likely a result of enhanced JNK activation. To directly determine whether S649 is modified in vivo, we generated phospho-specific Abs recognizing phospho-S649, and phospho-S657 as a positive control. Although phospho-S657 peaked and declined rapidly after Ag receptor stimulation, phospho-S649 occurred later and was maintained for a significantly longer period poststimulation in both B and T cells. Interestingly, phospho-S657 was completely abolished in PKCbeta-deficient B cells, whereas delayed phosphorylation at S649 was partially intact and depended, in part, upon novel PKC activity. Thus, distinct PKC-mediated CARMA1 phosphorylation events exert opposing effects on the activation status of CARMA1. We propose that early phosphorylation events at S657 and S564 promote the initial assembly of the CARMA1 signalosome, whereas later phosphorylation at S649 triggers CARMA1 down-regulation.
    MeSH term(s) Animals ; B-Lymphocytes/enzymology ; B-Lymphocytes/immunology ; Blotting, Western ; CARD Signaling Adaptor Proteins/immunology ; CARD Signaling Adaptor Proteins/metabolism ; Cell Line ; Chickens ; Down-Regulation ; Enzyme Activation ; Guanylate Cyclase/immunology ; Guanylate Cyclase/metabolism ; Humans ; I-kappa B Kinase/immunology ; I-kappa B Kinase/metabolism ; Immunoprecipitation ; MAP Kinase Kinase 4/immunology ; MAP Kinase Kinase 4/metabolism ; Mice ; Phosphorylation ; Protein Kinase C/immunology ; Protein Kinase C/metabolism ; Serine/metabolism ; Signal Transduction/immunology ; T-Lymphocytes/enzymology ; T-Lymphocytes/immunology
    Chemical Substances CARD Signaling Adaptor Proteins ; Serine (452VLY9402) ; I-kappa B Kinase (EC 2.7.11.10) ; Protein Kinase C (EC 2.7.11.13) ; MAP Kinase Kinase 4 (EC 2.7.12.2) ; CARD11 protein, human (EC 4.6.1.2) ; Guanylate Cyclase (EC 4.6.1.2)
    Language English
    Publishing date 2009-11-16
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 3056-9
    ISSN 1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
    ISSN (online) 1550-6606
    ISSN 0022-1767 ; 1048-3233 ; 1047-7381
    DOI 10.4049/jimmunol.0902438
    Database MEDical Literature Analysis and Retrieval System OnLINE

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