Structural Bases of PAS Domain-regulated Kinase (PASK) Activation in the Absence of Activation Loop Phosphorylation

• Published in: The Journal of biological chemistry Vol. 285; no. 52; pp. 41034 - 41043
• Main Authors: Kikani, Chintan K., Antonysamy, Stephen A., Bonanno, Jeffrey B., Romero, Rich, Zhang, Feiyu Fred, Russell, Marijane, Gheyi, Tarun, Iizuka, Miyo, Emtage, Spencer, Sauder, J. Michael, Turk, Benjamin E., Burley, Stephen K., Rutter, Jared
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 24.12.2010; American Society for Biochemistry and Molecular Biology
• Subjects: Activation Loop Phosphorylation; Cell Metabolism; Crystal Structure; Enzyme Activation - physiology; Humans; Kinase Structure; Metabolism; Mutagenesis, Site-Directed; PAS Domain; PASK; Phosphorylation; Protein Kinases; Protein Phosphorylation; Protein Structure and Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Protein-Serine-Threonine Kinases - chemistry; Protein-Serine-Threonine Kinases - genetics; Protein-Serine-Threonine Kinases - metabolism; Protein-serine/threonine Kinase; Structure-Activity Relationship; Crystal Structure; Protein Kinases; Cell Metabolism; Protein-serine/threonine Kinase; Kinase Structure; PAS Domain; Protein Phosphorylation; PASK; Metabolism; Activation Loop Phosphorylation

Per-Arnt-Sim (PAS) domain-containing protein kinase (PASK) is an evolutionary conserved protein kinase that coordinates cellular metabolism with metabolic demand in yeast and mammals. The molecular mechanisms underlying PASK regulation, however, remain unknown. Herein, we describe a crystal structur...