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Igor Cervenka - One of the best experts on this subject based on the ideXlab platform.

  • Mitogen-Activated Protein Kinases Promote WNT/beta-CateninSignaling via Phosphorylation of LRP6
    2011
    Co-Authors: Igor Cervenka, Gunnar Schulte, Joshua Wolf, Jan Masek, Pavel Krejci, William R. Wilcox, Alois Kozubík, Jsilvio Gutkind, Vítězslav Bryja
    Abstract:

    LDL-related Protein 6 (LRP6) is a coreceptor of WNTs and a key regulator of the WNT/beta-catenin pathway. Upon activation LRP6 is phosphorylated within its intracellular PPPS/TP motifs. On the basis of a kinome-wide siRNA screen and confirmative biochemical analysis, we show that several proline-directed Mitogen-Activated Protein Kinases (MAPKs), such as p38, ERK1/2 and JNK1 are sufficient and required for the phosphorylation of PPPS/TP motifs of LRP6. External stimuli, which control the activity of MAPKs, such as phorbolesters and fibroblast growth factor 2 (FGF2) control the choice of the LRP6-PPPS/TP kinase and regulate the amplitude of LRP6 phosphorylation and WNT/beta-catenin-dependent transcription. Our findings suggest that cells recruit not only one dedicated LRP6 kinase but rather select their LRP6 kinase depending on cell type and the external stimulus.

  • mitogen activated Protein Kinases promote wnt beta catenin signaling via phosphorylation of lrp6
    Molecular and Cellular Biology, 2011
    Co-Authors: Igor Cervenka, Joshua Wolf, Jan Masek, Pavel Krejci, William R. Wilcox, Alois Kozubík
    Abstract:

    LDL-related Protein 6 (LRP6) is a coreceptor of WNTs and a key regulator of the WNT/β-catenin pathway. Upon activation, LRP6 is phosphorylated within its intracellular PPPS/TP motifs. These phosphorylated motifs are required to recruit axin and to inhibit glycogen synthase kinase 3 (GSK3), two basic components of the β-catenin destruction complex. On the basis of a kinome-wide small interfering RNA (siRNA) screen and confirmative biochemical analysis, we show that several proline-directed Mitogen-Activated Protein Kinases (MAPKs), such as p38, ERK1/2, and JNK1 are sufficient and required for the phosphorylation of PPPS/TP motifs of LRP6. External stimuli, which control the activity of MAPKs, such as phorbol esters and fibroblast growth factor 2 (FGF2) control the choice of the LRP6-PPPS/TP kinase and regulate the amplitude of LRP6 phosphorylation and WNT/β-catenin-dependent transcription. Our findings suggest that cells not only recruit one dedicated LRP6 kinase but rather select their LRP6 kinase depending on cell type and the external stimulus. Moreover, direct phosphorylation of LRP6 by MAPKs provides a unique point for convergence between WNT/β-catenin signaling and mitogenic pathways.

  • Mitogen-Activated Protein Kinases promote WNT/beta-catenin signaling via phosphorylation of LRP6.
    Molecular and cellular biology, 2010
    Co-Authors: Igor Cervenka, Gunnar Schulte, Joshua Wolf, Jan Masek, Pavel Krejci, William R. Wilcox, Alois Kozubík, Jsilvio Gutkind, Vítězslav Bryja
    Abstract:

    LDL-related Protein 6 (LRP6) is a coreceptor of WNTs and a key regulator of the WNT/β-catenin pathway. Upon activation, LRP6 is phosphorylated within its intracellular PPPS/TP motifs. These phosphorylated motifs are required to recruit axin and to inhibit glycogen synthase kinase 3 (GSK3), two basic components of the β-catenin destruction complex. On the basis of a kinome-wide small interfering RNA (siRNA) screen and confirmative biochemical analysis, we show that several proline-directed Mitogen-Activated Protein Kinases (MAPKs), such as p38, ERK1/2, and JNK1 are sufficient and required for the phosphorylation of PPPS/TP motifs of LRP6. External stimuli, which control the activity of MAPKs, such as phorbol esters and fibroblast growth factor 2 (FGF2) control the choice of the LRP6-PPPS/TP kinase and regulate the amplitude of LRP6 phosphorylation and WNT/β-catenin-dependent transcription. Our findings suggest that cells not only recruit one dedicated LRP6 kinase but rather select their LRP6 kinase depending on cell type and the external stimulus. Moreover, direct phosphorylation of LRP6 by MAPKs provides a unique point for convergence between WNT/β-catenin signaling and mitogenic pathways.

Pavel Krejci - One of the best experts on this subject based on the ideXlab platform.

  • Mitogen-Activated Protein Kinases Promote WNT/beta-CateninSignaling via Phosphorylation of LRP6
    2011
    Co-Authors: Igor Cervenka, Gunnar Schulte, Joshua Wolf, Jan Masek, Pavel Krejci, William R. Wilcox, Alois Kozubík, Jsilvio Gutkind, Vítězslav Bryja
    Abstract:

    LDL-related Protein 6 (LRP6) is a coreceptor of WNTs and a key regulator of the WNT/beta-catenin pathway. Upon activation LRP6 is phosphorylated within its intracellular PPPS/TP motifs. On the basis of a kinome-wide siRNA screen and confirmative biochemical analysis, we show that several proline-directed Mitogen-Activated Protein Kinases (MAPKs), such as p38, ERK1/2 and JNK1 are sufficient and required for the phosphorylation of PPPS/TP motifs of LRP6. External stimuli, which control the activity of MAPKs, such as phorbolesters and fibroblast growth factor 2 (FGF2) control the choice of the LRP6-PPPS/TP kinase and regulate the amplitude of LRP6 phosphorylation and WNT/beta-catenin-dependent transcription. Our findings suggest that cells recruit not only one dedicated LRP6 kinase but rather select their LRP6 kinase depending on cell type and the external stimulus.

  • mitogen activated Protein Kinases promote wnt beta catenin signaling via phosphorylation of lrp6
    Molecular and Cellular Biology, 2011
    Co-Authors: Igor Cervenka, Joshua Wolf, Jan Masek, Pavel Krejci, William R. Wilcox, Alois Kozubík
    Abstract:

    LDL-related Protein 6 (LRP6) is a coreceptor of WNTs and a key regulator of the WNT/β-catenin pathway. Upon activation, LRP6 is phosphorylated within its intracellular PPPS/TP motifs. These phosphorylated motifs are required to recruit axin and to inhibit glycogen synthase kinase 3 (GSK3), two basic components of the β-catenin destruction complex. On the basis of a kinome-wide small interfering RNA (siRNA) screen and confirmative biochemical analysis, we show that several proline-directed Mitogen-Activated Protein Kinases (MAPKs), such as p38, ERK1/2, and JNK1 are sufficient and required for the phosphorylation of PPPS/TP motifs of LRP6. External stimuli, which control the activity of MAPKs, such as phorbol esters and fibroblast growth factor 2 (FGF2) control the choice of the LRP6-PPPS/TP kinase and regulate the amplitude of LRP6 phosphorylation and WNT/β-catenin-dependent transcription. Our findings suggest that cells not only recruit one dedicated LRP6 kinase but rather select their LRP6 kinase depending on cell type and the external stimulus. Moreover, direct phosphorylation of LRP6 by MAPKs provides a unique point for convergence between WNT/β-catenin signaling and mitogenic pathways.

  • Mitogen-Activated Protein Kinases promote WNT/beta-catenin signaling via phosphorylation of LRP6.
    Molecular and cellular biology, 2010
    Co-Authors: Igor Cervenka, Gunnar Schulte, Joshua Wolf, Jan Masek, Pavel Krejci, William R. Wilcox, Alois Kozubík, Jsilvio Gutkind, Vítězslav Bryja
    Abstract:

    LDL-related Protein 6 (LRP6) is a coreceptor of WNTs and a key regulator of the WNT/β-catenin pathway. Upon activation, LRP6 is phosphorylated within its intracellular PPPS/TP motifs. These phosphorylated motifs are required to recruit axin and to inhibit glycogen synthase kinase 3 (GSK3), two basic components of the β-catenin destruction complex. On the basis of a kinome-wide small interfering RNA (siRNA) screen and confirmative biochemical analysis, we show that several proline-directed Mitogen-Activated Protein Kinases (MAPKs), such as p38, ERK1/2, and JNK1 are sufficient and required for the phosphorylation of PPPS/TP motifs of LRP6. External stimuli, which control the activity of MAPKs, such as phorbol esters and fibroblast growth factor 2 (FGF2) control the choice of the LRP6-PPPS/TP kinase and regulate the amplitude of LRP6 phosphorylation and WNT/β-catenin-dependent transcription. Our findings suggest that cells not only recruit one dedicated LRP6 kinase but rather select their LRP6 kinase depending on cell type and the external stimulus. Moreover, direct phosphorylation of LRP6 by MAPKs provides a unique point for convergence between WNT/β-catenin signaling and mitogenic pathways.

Alois Kozubík - One of the best experts on this subject based on the ideXlab platform.

  • Mitogen-Activated Protein Kinases Promote WNT/beta-CateninSignaling via Phosphorylation of LRP6
    2011
    Co-Authors: Igor Cervenka, Gunnar Schulte, Joshua Wolf, Jan Masek, Pavel Krejci, William R. Wilcox, Alois Kozubík, Jsilvio Gutkind, Vítězslav Bryja
    Abstract:

    LDL-related Protein 6 (LRP6) is a coreceptor of WNTs and a key regulator of the WNT/beta-catenin pathway. Upon activation LRP6 is phosphorylated within its intracellular PPPS/TP motifs. On the basis of a kinome-wide siRNA screen and confirmative biochemical analysis, we show that several proline-directed Mitogen-Activated Protein Kinases (MAPKs), such as p38, ERK1/2 and JNK1 are sufficient and required for the phosphorylation of PPPS/TP motifs of LRP6. External stimuli, which control the activity of MAPKs, such as phorbolesters and fibroblast growth factor 2 (FGF2) control the choice of the LRP6-PPPS/TP kinase and regulate the amplitude of LRP6 phosphorylation and WNT/beta-catenin-dependent transcription. Our findings suggest that cells recruit not only one dedicated LRP6 kinase but rather select their LRP6 kinase depending on cell type and the external stimulus.

  • mitogen activated Protein Kinases promote wnt beta catenin signaling via phosphorylation of lrp6
    Molecular and Cellular Biology, 2011
    Co-Authors: Igor Cervenka, Joshua Wolf, Jan Masek, Pavel Krejci, William R. Wilcox, Alois Kozubík
    Abstract:

    LDL-related Protein 6 (LRP6) is a coreceptor of WNTs and a key regulator of the WNT/β-catenin pathway. Upon activation, LRP6 is phosphorylated within its intracellular PPPS/TP motifs. These phosphorylated motifs are required to recruit axin and to inhibit glycogen synthase kinase 3 (GSK3), two basic components of the β-catenin destruction complex. On the basis of a kinome-wide small interfering RNA (siRNA) screen and confirmative biochemical analysis, we show that several proline-directed Mitogen-Activated Protein Kinases (MAPKs), such as p38, ERK1/2, and JNK1 are sufficient and required for the phosphorylation of PPPS/TP motifs of LRP6. External stimuli, which control the activity of MAPKs, such as phorbol esters and fibroblast growth factor 2 (FGF2) control the choice of the LRP6-PPPS/TP kinase and regulate the amplitude of LRP6 phosphorylation and WNT/β-catenin-dependent transcription. Our findings suggest that cells not only recruit one dedicated LRP6 kinase but rather select their LRP6 kinase depending on cell type and the external stimulus. Moreover, direct phosphorylation of LRP6 by MAPKs provides a unique point for convergence between WNT/β-catenin signaling and mitogenic pathways.

  • Mitogen-Activated Protein Kinases promote WNT/beta-catenin signaling via phosphorylation of LRP6.
    Molecular and cellular biology, 2010
    Co-Authors: Igor Cervenka, Gunnar Schulte, Joshua Wolf, Jan Masek, Pavel Krejci, William R. Wilcox, Alois Kozubík, Jsilvio Gutkind, Vítězslav Bryja
    Abstract:

    LDL-related Protein 6 (LRP6) is a coreceptor of WNTs and a key regulator of the WNT/β-catenin pathway. Upon activation, LRP6 is phosphorylated within its intracellular PPPS/TP motifs. These phosphorylated motifs are required to recruit axin and to inhibit glycogen synthase kinase 3 (GSK3), two basic components of the β-catenin destruction complex. On the basis of a kinome-wide small interfering RNA (siRNA) screen and confirmative biochemical analysis, we show that several proline-directed Mitogen-Activated Protein Kinases (MAPKs), such as p38, ERK1/2, and JNK1 are sufficient and required for the phosphorylation of PPPS/TP motifs of LRP6. External stimuli, which control the activity of MAPKs, such as phorbol esters and fibroblast growth factor 2 (FGF2) control the choice of the LRP6-PPPS/TP kinase and regulate the amplitude of LRP6 phosphorylation and WNT/β-catenin-dependent transcription. Our findings suggest that cells not only recruit one dedicated LRP6 kinase but rather select their LRP6 kinase depending on cell type and the external stimulus. Moreover, direct phosphorylation of LRP6 by MAPKs provides a unique point for convergence between WNT/β-catenin signaling and mitogenic pathways.

William R. Wilcox - One of the best experts on this subject based on the ideXlab platform.

  • Mitogen-Activated Protein Kinases Promote WNT/beta-CateninSignaling via Phosphorylation of LRP6
    2011
    Co-Authors: Igor Cervenka, Gunnar Schulte, Joshua Wolf, Jan Masek, Pavel Krejci, William R. Wilcox, Alois Kozubík, Jsilvio Gutkind, Vítězslav Bryja
    Abstract:

    LDL-related Protein 6 (LRP6) is a coreceptor of WNTs and a key regulator of the WNT/beta-catenin pathway. Upon activation LRP6 is phosphorylated within its intracellular PPPS/TP motifs. On the basis of a kinome-wide siRNA screen and confirmative biochemical analysis, we show that several proline-directed Mitogen-Activated Protein Kinases (MAPKs), such as p38, ERK1/2 and JNK1 are sufficient and required for the phosphorylation of PPPS/TP motifs of LRP6. External stimuli, which control the activity of MAPKs, such as phorbolesters and fibroblast growth factor 2 (FGF2) control the choice of the LRP6-PPPS/TP kinase and regulate the amplitude of LRP6 phosphorylation and WNT/beta-catenin-dependent transcription. Our findings suggest that cells recruit not only one dedicated LRP6 kinase but rather select their LRP6 kinase depending on cell type and the external stimulus.

  • mitogen activated Protein Kinases promote wnt beta catenin signaling via phosphorylation of lrp6
    Molecular and Cellular Biology, 2011
    Co-Authors: Igor Cervenka, Joshua Wolf, Jan Masek, Pavel Krejci, William R. Wilcox, Alois Kozubík
    Abstract:

    LDL-related Protein 6 (LRP6) is a coreceptor of WNTs and a key regulator of the WNT/β-catenin pathway. Upon activation, LRP6 is phosphorylated within its intracellular PPPS/TP motifs. These phosphorylated motifs are required to recruit axin and to inhibit glycogen synthase kinase 3 (GSK3), two basic components of the β-catenin destruction complex. On the basis of a kinome-wide small interfering RNA (siRNA) screen and confirmative biochemical analysis, we show that several proline-directed Mitogen-Activated Protein Kinases (MAPKs), such as p38, ERK1/2, and JNK1 are sufficient and required for the phosphorylation of PPPS/TP motifs of LRP6. External stimuli, which control the activity of MAPKs, such as phorbol esters and fibroblast growth factor 2 (FGF2) control the choice of the LRP6-PPPS/TP kinase and regulate the amplitude of LRP6 phosphorylation and WNT/β-catenin-dependent transcription. Our findings suggest that cells not only recruit one dedicated LRP6 kinase but rather select their LRP6 kinase depending on cell type and the external stimulus. Moreover, direct phosphorylation of LRP6 by MAPKs provides a unique point for convergence between WNT/β-catenin signaling and mitogenic pathways.

  • Mitogen-Activated Protein Kinases promote WNT/beta-catenin signaling via phosphorylation of LRP6.
    Molecular and cellular biology, 2010
    Co-Authors: Igor Cervenka, Gunnar Schulte, Joshua Wolf, Jan Masek, Pavel Krejci, William R. Wilcox, Alois Kozubík, Jsilvio Gutkind, Vítězslav Bryja
    Abstract:

    LDL-related Protein 6 (LRP6) is a coreceptor of WNTs and a key regulator of the WNT/β-catenin pathway. Upon activation, LRP6 is phosphorylated within its intracellular PPPS/TP motifs. These phosphorylated motifs are required to recruit axin and to inhibit glycogen synthase kinase 3 (GSK3), two basic components of the β-catenin destruction complex. On the basis of a kinome-wide small interfering RNA (siRNA) screen and confirmative biochemical analysis, we show that several proline-directed Mitogen-Activated Protein Kinases (MAPKs), such as p38, ERK1/2, and JNK1 are sufficient and required for the phosphorylation of PPPS/TP motifs of LRP6. External stimuli, which control the activity of MAPKs, such as phorbol esters and fibroblast growth factor 2 (FGF2) control the choice of the LRP6-PPPS/TP kinase and regulate the amplitude of LRP6 phosphorylation and WNT/β-catenin-dependent transcription. Our findings suggest that cells not only recruit one dedicated LRP6 kinase but rather select their LRP6 kinase depending on cell type and the external stimulus. Moreover, direct phosphorylation of LRP6 by MAPKs provides a unique point for convergence between WNT/β-catenin signaling and mitogenic pathways.

Heribert Hirt - One of the best experts on this subject based on the ideXlab platform.

  • Quantitative Phosphoproteomic Analysis Reveals Shared and Specific Targets of Arabidopsis Mitogen-Activated Protein Kinases (MAPKs) MPK3, MPK4, and MPK6
    Molecular and Cellular Proteomics, 2018
    Co-Authors: Naganand Rayapuram, Heribert Hirt, Jean Bigeard, Hanna Alhoraibi, Ludovic Bonhomme, Anne-marie Hesse, Joelle Vinh, Delphine Pflieger
    Abstract:

    In Arabidopsis, Mitogen-Activated Protein Kinases MPK3, MPK4, and MPK6 constitute essential relays for a variety of functions including cell division, development and innate immunity. Although some substrates of MPK3, MPK4 and MPK6 have been identified, the picture is still far from complete. To identify substrates of these MAPKs likely involved in cell division, growth and development we compared the phosphoproteomes of wild-type and mpk3, mpk4, and mpk6. To study the function of these MAPKs in innate immunity, we analyzed their phosphoproteomes following microbe-associated molecular pattern (MAMP) treatment. Partially overlapping substrates were retrieved for all three MAPKs, showing target specificity to one, two or all three MAPKs in different biological processes. More precisely, our results illustrate the fact that the entity to be defined as a specific or a shared substrate for MAPKs is not a phosphoProtein but a particular (S/T) P phosphorylation site in a given Protein. One hundred fifty-two peptides were identified to be differentially phosphorylated in response to MAMP treatment and/or when compared between genotypes and 70 of them could be classified as putative MAPK targets. Biochemical analysis of a number of putative MAPK substrates by phosphorylation and interaction assays confirmed the global phosphoproteome approach. Our study also expands the set of MAPK substrates to involve other Protein Kinases, including calcium-dependent (CDPK) and sugar nonfermenting (SnRK) Protein Kinases.

  • Signaling mechanisms in pattern-triggered immunity (PTI)
    Molecular Plant, 2015
    Co-Authors: Jean Bigeard, Jean Colcombet, Heribert Hirt
    Abstract:

    In nature, plants constantly have to face pathogen attacks. However, plant disease rarely occurs due to efficient immune systems possessed by the host plants. Pathogens are perceived by two different recognition systems that initiate the so-called pattern-triggered immunity (PTI) and effector-triggered immunity (ETI), both of which are accompanied by a set of induced defenses that usually repel pathogen attacks. Here we discuss the complex network of signaling pathways occurring during PTI, focusing on the involvement of Mitogen-Activated Protein Kinases.

  • Identification of constitutively active AtMPK6 mutants using a functional screen in saccharomyces cerevisiae
    2014
    Co-Authors: Elodie Hudik, Heribert Hirt, Souha Berriri, Jean Colcombet
    Abstract:

    MAPK (Mitogen-Activated Protein Kinases) mutants which are active independently of phosphorylation by upstream MAPK Kinases (MAPKKs) help to clarify signal transduction processes through MAPK modules and provide a useful tool to understand MAPK roles in the cell. The identification of such mutations is tricky. In this chapter, we provide a detailed protocol for their screening, taking advantage of a functional expression assay in yeast.

  • improvement of stress tolerance in plants by genetic manipulation of mitogen activated Protein Kinases
    Biotechnology Advances, 2013
    Co-Authors: Olga Samajova, Heribert Hirt, Ondřej Plihal, Mohamed S Alyousif, Jozef Samaj
    Abstract:

    Plant stress tolerance depends on many factors among which signaling by Mitogen-Activated Protein-kinase (MAPK) modules plays a crucial role. Reversible phosphorylation of MAPKs, their upstream activators and downstream targets such as transcription factors can trigger a myriad of transcriptomic, cellular and physiological responses. Genetic manipulation of abundance and/or activity of some of these modular MAPK components can lead to better stress tolerance in Arabidopsis and crop plant species such as tobacco and cereals. The main focus of this review is devoted to the MAPK-related signaling components which show the most promising biotechnological potential. Additionally, recent studies identified MAPK components to be involved both in plant development as well as in stress responses, suggesting that these processes are tightly linked in plants.

  • Improvement of stress tolerance in plants by genetic manipulation of Mitogen-Activated Protein Kinases
    Biotechnology Advances, 2013
    Co-Authors: Ondřej Plihal, Heribert Hirt, Mohamed Al-yousif, Jozef Samaj
    Abstract:

    Plant stress tolerance depends on many factors among which signaling by Mitogen-Activated Protein-kinase (MAPK) modules plays a crucial role. Reversible phosphorylation of MAPKs, their upstream activators and downstream targets such as transcription factors can trigger a myriad of transcriptomic, cellular and physiological responses. Genetic manipulation of abundance and/or activity of some of these modular MAPK components can lead to better stress tolerance in Arabidopsis and crop plant species such as tobacco and cereals. The main focus of this review is devoted to the MAPK-related signaling components which show the most promising biotechnological potential. Additionally, recent studies identified MAPK components to be involved both in plant development as well as in stress responses, suggesting that these processes are tightly linked in plants. (c) 2011 Elsevier Inc. All rights reserved.