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    Mapkapk2 MAP kinase-activated protein kinase 2 [ Mus musculus (house mouse) ]

    Gene ID: 17164, updated on 13-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Increased Activity of MAPKAPK2 within Mesenchymal Cells as a Target for Inflammation-Associated Fibrosis in Crohn's Disease.

    Increased Activity of MAPKAPK2 within Mesenchymal Cells as a Target for Inflammation-Associated Fibrosis in Crohn's Disease.
    Chulkina M, Rohmer C, McAninch S, Panganiban RP, Villéger R, Portolese A, Ciocirlan J, Yang W, Cohen C, Koltun W, Valentine JF, Cong Y, Yochum G, Beswick EJ, Pinchuk IV.

    09/13/2024
    CD93 Ameliorates Diabetic Wounds by Promoting Angiogenesis via the p38MAPK/MK2/HSP27 Axis.

    CD93 Ameliorates Diabetic Wounds by Promoting Angiogenesis via the p38MAPK/MK2/HSP27 Axis.
    Xu Y, Jia Y, Wu N, Wang J, He L, Yang D.

    11/15/2023
    MK2 drives progression of pancreas and colon cancers by suppressing CD8[+] T cell cytotoxic function and is a potential immunotherapy target.

    MK2 drives progression of pancreas and colon cancers by suppressing CD8(+) T cell cytotoxic function and is a potential immunotherapy target.
    Jacenik D, Lebish EJ, Beswick EJ., Free PMC Article

    07/12/2023
    Promyelocytic leukemia protein targets MK2 to promote cytotoxicity.

    Promyelocytic leukemia protein targets MK2 to promote cytotoxicity.
    Chen IT, Chen HC, Lo YH, Lai PY, Hsieh FY, Wu YH, Shih HM, Lai MZ., Free PMC Article

    03/19/2022
    MK2 promotes Tfcp2l1 degradation via beta-TrCP ubiquitin ligase to regulate mouse embryonic stem cell self-renewal.

    MK2 promotes Tfcp2l1 degradation via β-TrCP ubiquitin ligase to regulate mouse embryonic stem cell self-renewal.
    Zhang Y, Ding H, Wang X, Wang X, Wan S, Xu A, Gan R, Ye SD.

    02/19/2022
    MAPKAP Kinase-2 Drives Expression of Angiogenic Factors by Tumor-Associated Macrophages in a Model of Inflammation-Induced Colon Cancer.

    MAPKAP Kinase-2 Drives Expression of Angiogenic Factors by Tumor-Associated Macrophages in a Model of Inflammation-Induced Colon Cancer.
    Suarez-Lopez L, Kong YW, Sriram G, Patterson JC, Rosenberg S, Morandell S, Haigis KM, Yaffe MB., Free PMC Article

    06/26/2021
    IL-33-activated murine mast cells control the dichotomy between RORgammat(+) and Helios(+) Tregs via the MK2/3-mediated IL-6 production in vitro

    IL-33-activated murine mast cells control the dichotomy between RORγt(+) and Helios(+) T(regs) via the MK2/3-mediated IL-6 production in vitro.
    Andreas N, Weber F, Meininger I, Templin N, Gaestel M, Kamradt T, Drube S.

    05/30/2020
    The MK2/3 are the only LPS-induced kinases for S52 and S178 of TTP and the role of MK2 and MK3 in the regulation of TNF biosynthesis is not restricted to phosphorylation of TTP at S52/S178 but includes independent processes, which could involve other TTP phosphorylations.

    The Role of TTP Phosphorylation in the Regulation of Inflammatory Cytokine Production by MK2/3.
    Ronkina N, Shushakova N, Tiedje C, Yakovleva T, Tollenaere MAX, Scott A, Batth TS, Olsen JV, Helmke A, Bekker-Jensen SH, Clark AR, Kotlyarov A, Gaestel M.

    05/23/2020
    MK2 is a serine/threonine kinase that functions downstream of p38 stress-activated mitogen-activated protein kinase with a role in experimental colitis

    Substrate-based kinase activity inference identifies MK2 as driver of colitis.
    Strasser SD, Ghazi PC, Starchenko A, Boukhali M, Edwards A, Suarez-Lopez L, Lyons J, Changelian PS, Monahan JB, Jacobsen J, Brubaker DK, Joughin BA, Yaffe MB, Haas W, Lauffenburger DA, Haigis KM., Free PMC Article

    04/18/2020
    This is the first study to demonstrate the critical role of the MK2 pathway in chemokine production, macrophage influx, macrophage function, and tumor growth.

    MK2 Regulates Macrophage Chemokine Activity and Recruitment to Promote Colon Tumor Growth.
    Phinney BB, Ray AL, Peretti AS, Jerman SJ, Grim C, Pinchuk IV, Beswick EJ., Free PMC Article

    10/5/2019
    MK2 augments hepatic I/R injury and induces ROS production.

    A Role for MK2 in Enhancing Neutrophil-Derived ROS Production and Aggravating Liver Ischemia/Reperfusion Injury.
    Sun L, Wu Q, Nie Y, Cheng N, Wang R, Wang G, Zhang D, He H, Ye RD, Qian F., Free PMC Article

    10/5/2019
    results suggested that MK2 boosts LPS-induced macrophage activation and ALI via increasing activation of CREB and consequently, the expression of Lin28 and downregulation of let-7e.

    MK2 mediates macrophage activation and acute lung injury by regulating let-7e miRNA.
    Wu Y, He H, Ding Y, Liu S, Zhang D, Wang J, Jiang H, Zhang D, Sun L, Ye RD, Qian F.

    07/6/2019
    MK2 deletion in CD11c(+) cells led to an expansion of stimulatory CD103(+) DCs, mounting a potent CD8(+) T cell response that resulted in elimination of highly aggressive B16-F10 tumours upon toll-like receptor (TLR) activation in the presence of tumour antigen.

    Loss of MAPK-activated protein kinase 2 enables potent dendritic cell-driven anti-tumour T cell response.
    Soukup K, Halfmann A, Dillinger B, Poyer F, Martin K, Blauensteiner B, Kauer M, Kuttke M, Schabbauer G, Dohnal AM., Free PMC Article

    06/29/2019
    A novel role of Hsp70 in regulating myoblast differentiation by interacting with MK2 to stabilize p38MAPK.

    Hsp70 Interacts with Mitogen-Activated Protein Kinase (MAPK)-Activated Protein Kinase 2 To Regulate p38MAPK Stability and Myoblast Differentiation during Skeletal Muscle Regeneration.
    Fan W, Gao XK, Rao XS, Shi YP, Liu XC, Wang FY, Liu YF, Cong XX, He MY, Xu SB, Shen WL, Shen Y, Yan SG, Luo Y, Low BC, Ouyang H, Bao Z, Zheng LL, Zhou YT., Free PMC Article

    06/15/2019
    The importance of MK2 in driving proinflammatory cytokine production, its relevance to in vivo tumor proliferation and invasion.

    Inhibition of MK2 suppresses IL-1β, IL-6, and TNF-α-dependent colorectal cancer growth.
    Ray AL, Berggren KL, Restrepo Cruz S, Gan GN, Beswick EJ., Free PMC Article

    11/3/2018
    MK2 promotes polarization of tumor-associated macrophages into protumorigenic, proangiogenic M2-like macrophages.

    MK2 contributes to tumor progression by promoting M2 macrophage polarization and tumor angiogenesis.
    Suarez-Lopez L, Sriram G, Kong YW, Morandell S, Merrick KA, Hernandez Y, Haigis KM, Yaffe MB., Free PMC Article

    08/18/2018
    Phosphorylation of inhibitory PAS domain protein (IPAS) at Ser184 by MAPK-activated protein kinase 2 (MK2 or MAPKAPK2) enhances the proapoptotic function of IPAS.

    Increase in proapoptotic activity of inhibitory PAS domain protein via phosphorylation by MK2.
    Kasai S, Richardson MJE, Torii S, Yasumoto KI, Shima H, Igarashi K, Itoh K, Sogawa K, Murayama K.

    12/30/2017
    p38MAPK/MK2 phosphorylation of RIPK1 is a crucial checkpoint for cell fate in inflammation and infection that determines the outcome of bacteria-host cell interaction.

    p38(MAPK)/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection.
    Menon MB, Gropengießer J, Fischer J, Novikova L, Deuretzbacher A, Lafera J, Schimmeck H, Czymmeck N, Ronkina N, Kotlyarov A, Aepfelbacher M, Gaestel M, Ruckdeschel K.

    10/28/2017
    MK2-mediated RIPK1 phosphorylation is an important molecular mechanism limiting the sensitivity of the cells to the cytotoxic effects of TNF.

    MK2 phosphorylation of RIPK1 regulates TNF-mediated cell death.
    Dondelinger Y, Delanghe T, Rojas-Rivera D, Priem D, Delvaeye T, Bruggeman I, Van Herreweghe F, Vandenabeele P, Bertrand MJM.

    10/28/2017
    MK2-mediated phosphorylation of RIPK1 serves as a checkpoint within the TNF signaling pathway that integrates cell survival and cytokine production.

    MK2 Phosphorylates RIPK1 to Prevent TNF-Induced Cell Death.
    Jaco I, Annibaldi A, Lalaoui N, Wilson R, Tenev T, Laurien L, Kim C, Jamal K, Wicky John S, Liccardi G, Chau D, Murphy JM, Brumatti G, Feltham R, Pasparakis M, Silke J, Meier P., Free PMC Article

    09/23/2017
    this study shows that the loss of MK2 in mast cells decreases the IL-33-induced leukocyte recruitment and the resulting skin inflammation

    MK2/3 Are Pivotal for IL-33-Induced and Mast Cell-Dependent Leukocyte Recruitment and the Resulting Skin Inflammation.
    Drube S, Kraft F, Dudeck J, Müller AL, Weber F, Göpfert C, Meininger I, Beyer M, Irmler I, Häfner N, Schütz D, Stumm R, Yakovleva T, Gaestel M, Dudeck A, Kamradt T.

    08/19/2017
    MK2 signaling differentially regulated CCL3 and CCL4.

    Mitogen-Activated Protein Kinase 2 Signaling Shapes Macrophage Plasticity in Aggregatibacter actinomycetemcomitans-Induced Bone Loss.
    Herbert BA, Steinkamp HM, Gaestel M, Kirkwood KL., Free PMC Article

    05/20/2017
    In silico analyses and experimental validation demonstrated that the kinase activity of p38(MAPK) determines signal amplitude, whereas phosphatase activity affects both signal amplitude and duration. p38(MAPK) and MK2 concentrations and responsiveness toward IL-1beta were quantitatively compared between hepatocytes and macrophages

    IL-1β-induced and p38(MAPK)-dependent activation of the mitogen-activated protein kinase-activated protein kinase 2 (MK2) in hepatocytes: Signal transduction with robust and concentration-independent signal amplification.
    Kulawik A, Engesser R, Ehlting C, Raue A, Albrecht U, Hahn B, Lehmann WD, Gaestel M, Klingmüller U, Häussinger D, Timmer J, Bode JG., Free PMC Article

    04/29/2017
    MK2-activating peptide (MK2-AP) blocks the effects of anthrax lethal toxin on endothelial barriers in cultured cells and reduces pulmonary vascular leak in rats.

    Anthrax lethal toxin-induced lung injury and treatment by activating MK2.
    Liu T, Warburton RR, Hill NS, Kayyali US., Free PMC Article

    06/11/2016
    MK2 regulates postnatal arteriogenesis by controlling vascular recruitment of monocytes/macrophages in dual manner: regulation of endothelial MCP-1 expression in response to hemodynamic and inflammatory forces as well as MCP-1 dependent monocyte migration

    MAP-Kinase Activated Protein Kinase 2 Links Endothelial Activation and Monocyte/macrophage Recruitment in Arteriogenesis.
    Limbourg A, von Felden J, Jagavelu K, Krishnasamy K, Napp LC, Kapopara PR, Gaestel M, Schieffer B, Bauersachs J, Limbourg FP, Bavendiek U., Free PMC Article

    06/4/2016
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