Phosphorylation of the kinase interaction motif in Mitogen-activated Protein (MAP) kinase phosphatase-4 mediates cross-talk between protein kinase A and MAP kinase signaling pathways

Journal of Biological Chemistry

Volumn 286, Issue 44, 2011, Pages 38018-38026

  Dickinson, Robin J ^a   Delavaine, Laurent ^a   Cejudo Marín, Rocío ^b   Stewart, Graeme ^a   Staples, Christopher J ^a   Didmon, Mark P ^a   Trinidad, Antonio Garcia ^c   Alonso, Andrés ^c   Pulido, Rafael ^b   Keyse, Stephen M ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

^b CENTRO DE INVESTIGACIÓN PRÍNCIPE FELIPE   (Spain)

^c UNIVERSITY OF VALLADOLID   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

FORSKOLIN; GLUTAMIC ACID; IN-VITRO; IN-VIVO; MAP KINASE; MAP KINASE SIGNALING; MAPK SIGNALING; MITOGEN ACTIVATED PROTEIN KINASE; NON-CATALYTIC; PHOSPHORYLATION SITES; PROTEIN KINASE A;

AMINO ACIDS; CATALYST ACTIVITY; CROSSTALK; PHOSPHATASES; PROTEINS; SIGNALING; TISSUE;

PHOSPHORYLATION;

ALANINE; ARGININE; CYCLIC AMP DEPENDENT PROTEIN KINASE; FORSKOLIN; GLUTAMIC ACID; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 14; MITOGEN ACTIVATED PROTEIN KINASE PHOSPHATASE; MITOGEN ACTIVATED PROTEIN KINASE PHOSPHATASE 4; SERINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CATALYSIS; CONTROLLED STUDY; CYTOPLASM; EMBRYO; ENZYME BINDING; ENZYME INACTIVATION; ENZYME PHOSPHORYLATION; ENZYME SUBSTRATE; GENE MUTATION; IN VITRO STUDY; IN VIVO STUDY; MOUSE; NONHUMAN; PLACENTA; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION;

AMINO ACID MOTIFS; ANIMALS; CATALYSIS; CATALYTIC DOMAIN; CERCOPITHECUS AETHIOPS; COS CELLS; CYCLIC AMP-DEPENDENT PROTEIN KINASES; DUAL-SPECIFICITY PHOSPHATASES; HUMANS; MICE; MITOGEN-ACTIVATED PROTEIN KINASE PHOSPHATASES; P38 MITOGEN-ACTIVATED PROTEIN KINASES; PHOSPHORYLATION; RECOMBINANT PROTEINS; SIGNAL TRANSDUCTION;

EID: 80055079454     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.255844     Document Type: Article

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