A conserved docking motif in MAP kinases common to substrates, activators and regulators

• Published in: Nature cell biology Vol. 2; no. 2; pp. 110 - 116
• Main Authors: Nishida, Eisuke, Tanoue, Takuji, Adachi, Makoto, Moriguchi, Tetsuo
• Format: Journal Article
• Language: English
• Published: England Nature Publishing Group 01.02.2000
• Subjects: Amino Acid Motifs; Amino Acid Sequence; Amino acids; Binding Sites; Binding sites (Biochemistry); Calcium-Calmodulin-Dependent Protein Kinases - metabolism; Cellular signal transduction; Conserved Sequence; Dual Specificity Phosphatase 6; Enzymes; Kinases; MAP Kinase Kinase 1; Mitogen-Activated Protein Kinase 1 - metabolism; Mitogen-Activated Protein Kinase Kinases - metabolism; Mitogen-Activated Protein Kinases - metabolism; Models, Molecular; Molecular Sequence Data; p38 Mitogen-Activated Protein Kinases; Phosphatase; Phosphorylation; Physiological aspects; Protein Binding; Protein kinases; Protein Tyrosine Phosphatases - metabolism; Protein-Serine-Threonine Kinases - metabolism; Proteins; Signal transduction; Transcription factors

Mitogen-activated protein kinases (MAPKs) are specifically phosphorylated and activated by the MAPK kinases, phosphorylate various targets such as MAPK-activated protein kinases and transcription factors, and are inactivated by specific phosphatases. Recently, docking interactions via the non-cataly...