Phosphorylation and Dimerization Regulate Nucleocytoplasmic Shuttling of Mammalian STE20-like Kinase (MST)

• Published in: The Journal of biological chemistry Vol. 277; no. 14; pp. 12351 - 12358
• Main Authors: Lee, Kyung-Kwon, Yonehara, Shin
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 05.04.2002; American Society for Biochemistry and Molecular Biology
• Subjects: 3T3 Cells; Active Transport, Cell Nucleus; Amino Acid Sequence; Animals; Antibiotics, Antineoplastic - pharmacology; Apoptosis; Blotting, Western; Cell Nucleus - metabolism; Cloning, Molecular; Cytoplasm - metabolism; Dimerization; Dose-Response Relationship, Drug; Enzyme Activation; Fatty Acids, Unsaturated - pharmacology; Genetic Vectors; HeLa Cells; Humans; MAP Kinase Kinase Kinases; Mice; Microscopy, Fluorescence; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Okadaic Acid - pharmacology; Phosphoric Monoester Hydrolases - antagonists & inhibitors; Phosphorylation; Precipitin Tests; Protein Binding; Protein Structure, Tertiary; Protein Transport; Protein-Serine-Threonine Kinases - chemistry; Protein-Serine-Threonine Kinases - metabolism; Sequence Homology, Amino Acid; Signal Transduction; Time Factors; Transfection

Mammalian STE20-like kinase (MST) is a member of the yeast STE20-related kinase family and proteolytically activated by caspase during apoptosis. However, its other cellular functions are not known, including its activation mechanism, substrate(s), and subcellular localization. In this report, using...