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10.1186/s12964-015-0100-3 http://scihub22266oqcxt.onion/10.1186/s12964-015-0100-3 C4390099!4390099!25889880     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Commun+Signal 2015 ; 13 (ä): ä Nephropedia Template TP {{tp|p=25889880|t=2015. Novel Protein kinase C ?: Coronin 1A complex in T lymphocytes |pdf=|usr=}}{{25889880}} gab.com Text Novel Protein kinase C : Coronin 1A complex in T lymphocytes JO: Cell Commun Signal http://www.kidney.de/pget.php?&tw=1&pmid=25889880 #FOAvip Background: Protein kinase C-? (PKC?) plays an important role in signal transduction down-stream of the T cell receptor and T cells deficient of PKC? show impaired NF-?B as well as NFAT/AP-1 activation resulting in strongly decreased IL-2 expression and proliferation. However, it is not yet entirely clear, how the function of PKC? - upon T cell activation - is regulated on a molecular level. Findings: Employing a yeast two-hybrid screen and co-immunoprecipitation analyses, we here identify coronin 1A (Coro1A) as a novel PKC?-interacting protein. We show that the NH2-terminal WD40 domains of Coro1A and the C2-like domain of PKC? are sufficient for the interaction. Furthermore, we confirm a physical interaction by GST-Coro1A mediated pull-down of endogenous PKC? protein. Functionally, wild-type but not Coro1A lacking its actin-binding domain negatively interferes with PKC?-dependent NF-?B, Cyclin D1 and IL-2 transactivation when analysed with luciferase promoter activation assays in Jurkat T cells. This could be phenocopied by pharmacological inhibitors of actin polymerization and PKC, respectively. Mechanistically, Coro1A overexpression attenuates both lipid raft and plasma membrane recruitment of PKC? in CD3/CD28-activated T cells.Using primary CD3+ T cells, we observed that (opposite to PKC?) Coro1A does not localize preferentially to the immunological synapse. In addition, we show that CD3+ T cells isolated from Coro1A-deficient mice show impaired IKK/NF-?B transactivation. Conclusions: Together, these findings both in Jurkat T cells as well as in primary T cells indicate a regulatory role of Coro1A on PKC? recruitment and function downstream of the TCR leading to NF-?B transactivation. Electronic supplementary material: The online version of this article (doi:10.1186/s12964-015-0100-3) contains supplementary material, which is available to authorized users. Twit Text FOAVip Novel Protein kinase C : Coronin 1A complex in T lymphocytes ????Cell Commun Signal http://www.kidney.de/pget.php?&tw=1&pmid=25889880 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25889880 #FOAvip English Wikipedia <ref>{{Cite pmid|25889880}}</ref> Novel Protein kinase C ?: Coronin 1A complex in T lymphocytes #MMPMID25889880 Siegmund K; Thuille N; Posch N; Fresser F; Baier G Cell Commun Signal 2015[]; 13 (ä): ä PMID25889880show ga Background: Protein kinase C-? (PKC?) plays an important role in signal transduction down-stream of the T cell receptor and T cells deficient of PKC? show impaired NF-?B as well as NFAT/AP-1 activation resulting in strongly decreased IL-2 expression and proliferation. However, it is not yet entirely clear, how the function of PKC? - upon T cell activation - is regulated on a molecular level. Findings: Employing a yeast two-hybrid screen and co-immunoprecipitation analyses, we here identify coronin 1A (Coro1A) as a novel PKC?-interacting protein. We show that the NH2-terminal WD40 domains of Coro1A and the C2-like domain of PKC? are sufficient for the interaction. Furthermore, we confirm a physical interaction by GST-Coro1A mediated pull-down of endogenous PKC? protein. Functionally, wild-type but not Coro1A lacking its actin-binding domain negatively interferes with PKC?-dependent NF-?B, Cyclin D1 and IL-2 transactivation when analysed with luciferase promoter activation assays in Jurkat T cells. This could be phenocopied by pharmacological inhibitors of actin polymerization and PKC, respectively. Mechanistically, Coro1A overexpression attenuates both lipid raft and plasma membrane recruitment of PKC? in CD3/CD28-activated T cells.Using primary CD3+ T cells, we observed that (opposite to PKC?) Coro1A does not localize preferentially to the immunological synapse. In addition, we show that CD3+ T cells isolated from Coro1A-deficient mice show impaired IKK/NF-?B transactivation. Conclusions: Together, these findings both in Jurkat T cells as well as in primary T cells indicate a regulatory role of Coro1A on PKC? recruitment and function downstream of the TCR leading to NF-?B transactivation. Electronic supplementary material: The online version of this article (doi:10.1186/s12964-015-0100-3) contains supplementary material, which is available to authorized users. äNovel Protein kinase C ?: Coronin 1A complex in T lymphocytes (epmc).pdf DeepDyve Pubget Overpricing