MAP Kinase Interactions
Published by Anonymous on 2007/9/28 (2011 reads)
1: Methods. 2006 Nov;40(3):213-23.
Analysis of mitogen-activated protein kinase activation and interactions with regulators and substrates.
Bardwell L, Shah K.
Department of Developmental and Cell Biology, University of California, Irvine, CA 92697, USA. bardwell@uci.edu
Mitogen-activated protein kinase (MAPK) cascades are ubiquitous signal transduction modules in eukaryotes that are of great interest and importance. Here, we summarize some useful methods for the analysis of MAPK signaling, including methods to (1) detect MAPK activation in cells, with an emphasis on using phosphorylation-state-specific antibodies raised against mammalian phosphopeptide sequences to detect the activation of MAPKs in other species; (2) estimate the cellular concentrations of MAPKs and other proteins of interest; (3) detect and quantify the stable physical association of MAPKs with their substrates and regulators, and estimate the relevant dissociation constants; (4) delineate the MAPK-binding regions or domains of MAPK-interacting proteins, with particular emphasis on the identification and verification of MAPK-docking sites. These procedures are broadly applicable to many organisms, including both yeast and mammalian cells.
Publication Types:
Research Support, N.I.H., Extramural
Review
PMID: 16884917 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Pharmacol Ther. 2002 Feb-Mar;93(2-3):193-202.
Docking interactions in the mitogen-activated protein kinase cascades.
Tanoue T, Nishida E.
Department of Cell and Developmental Biology, Graduate School of Biostudies, Kyoto University, Sakyo-ku, 606-8502, Kyoto, Japan.
Regulation of cellular functions and responses utilizes a number of the signal transduction pathways. Each pathway should transduce signals with high efficiency and fidelity to avoid unnecessary crosstalks. The mitogen-activated protein kinase (MAPK) cascades regulate a wide variety of cellular functions, including cell proliferation, differentiation, and stress responses. MAPK is activated by MAPK kinase; phosphorylates various targets, including transcription factors and MAPK-activated protein kinases; and is inactivated by several phosphatases. Recent studies have provided a cue to understand the molecular mechanism underlying the signal transduction through the MAPK cascades. In the MAPK cascades, docking interactions, which are achieved through a site outside the catalytic domain of MAPKs, regulate the efficiency and specificity of the enzymatic reactions. The docking interaction is different from a transient enzyme-substrate interaction through the active center. It has been shown that activators, substrates, and inactivators of MAPKs utilize a common site on MAPKs in the docking interaction. Then, the docking interaction may regulate not only the efficiency and specificity of the cascades, but also the ordered and integrated signaling.
Publication Types:
Review
PMID: 12191611 [PubMed - indexed for MEDLINE]
Analysis of mitogen-activated protein kinase activation and interactions with regulators and substrates.
Bardwell L, Shah K.
Department of Developmental and Cell Biology, University of California, Irvine, CA 92697, USA. bardwell@uci.edu
Mitogen-activated protein kinase (MAPK) cascades are ubiquitous signal transduction modules in eukaryotes that are of great interest and importance. Here, we summarize some useful methods for the analysis of MAPK signaling, including methods to (1) detect MAPK activation in cells, with an emphasis on using phosphorylation-state-specific antibodies raised against mammalian phosphopeptide sequences to detect the activation of MAPKs in other species; (2) estimate the cellular concentrations of MAPKs and other proteins of interest; (3) detect and quantify the stable physical association of MAPKs with their substrates and regulators, and estimate the relevant dissociation constants; (4) delineate the MAPK-binding regions or domains of MAPK-interacting proteins, with particular emphasis on the identification and verification of MAPK-docking sites. These procedures are broadly applicable to many organisms, including both yeast and mammalian cells.
Publication Types:
Research Support, N.I.H., Extramural
Review
PMID: 16884917 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Pharmacol Ther. 2002 Feb-Mar;93(2-3):193-202.
Docking interactions in the mitogen-activated protein kinase cascades.
Tanoue T, Nishida E.
Department of Cell and Developmental Biology, Graduate School of Biostudies, Kyoto University, Sakyo-ku, 606-8502, Kyoto, Japan.
Regulation of cellular functions and responses utilizes a number of the signal transduction pathways. Each pathway should transduce signals with high efficiency and fidelity to avoid unnecessary crosstalks. The mitogen-activated protein kinase (MAPK) cascades regulate a wide variety of cellular functions, including cell proliferation, differentiation, and stress responses. MAPK is activated by MAPK kinase; phosphorylates various targets, including transcription factors and MAPK-activated protein kinases; and is inactivated by several phosphatases. Recent studies have provided a cue to understand the molecular mechanism underlying the signal transduction through the MAPK cascades. In the MAPK cascades, docking interactions, which are achieved through a site outside the catalytic domain of MAPKs, regulate the efficiency and specificity of the enzymatic reactions. The docking interaction is different from a transient enzyme-substrate interaction through the active center. It has been shown that activators, substrates, and inactivators of MAPKs utilize a common site on MAPKs in the docking interaction. Then, the docking interaction may regulate not only the efficiency and specificity of the cascades, but also the ordered and integrated signaling.
Publication Types:
Review
PMID: 12191611 [PubMed - indexed for MEDLINE]
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