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

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Published inThe 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
LanguageEnglish
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
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Abstract 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 structure of the kinase domain of human PASK, which provides insights into the regulatory mechanisms governing catalysis. We show that the kinase domain adopts an active conformation and has catalytic activity in vivo and in vitro in the absence of activation loop phosphorylation. Using site-directed mutagenesis and structural comparison with active and inactive kinases, we identified several key structural features in PASK that enable activation loop phosphorylation-independent activity. Finally, we used combinatorial peptide library screening to determine that PASK prefers basic residues at the P-3 and P-5 positions in substrate peptides. Our results describe the key features of the PASK structure and how those features are important for PASK activity and substrate selection.
AbstractList 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 structure of the kinase domain of human PASK, which provides insights into the regulatory mechanisms governing catalysis. We show that the kinase domain adopts an active conformation and has catalytic activity in vivo and in vitro in the absence of activation loop phosphorylation. Using site-directed mutagenesis and structural comparison with active and inactive kinases, we identified several key structural features in PASK that enable activation loop phosphorylation-independent activity. Finally, we used combinatorial peptide library screening to determine that PASK prefers basic residues at the P-3 and P-5 positions in substrate peptides. Our results describe the key features of the PASK structure and how those features are important for PASK activity and substrate selection.
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 structure of the kinase domain of human PASK, which provides insights into the regulatory mechanisms governing catalysis. We show that the kinase domain adopts an active conformation and has catalytic activity in vivo and in vitro in the absence of activation loop phosphorylation. Using site-directed mutagenesis and structural comparison with active and inactive kinases, we identified several key structural features in PASK that enable activation loop phosphorylation-independent activity. Finally, we used combinatorial peptide library screening to determine that PASK prefers basic residues at the P-3 and P-5 positions in substrate peptides. Our results describe the key features of the PASK structure and how those features are important for PASK activity and substrate selection.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 structure of the kinase domain of human PASK, which provides insights into the regulatory mechanisms governing catalysis. We show that the kinase domain adopts an active conformation and has catalytic activity in vivo and in vitro in the absence of activation loop phosphorylation. Using site-directed mutagenesis and structural comparison with active and inactive kinases, we identified several key structural features in PASK that enable activation loop phosphorylation-independent activity. Finally, we used combinatorial peptide library screening to determine that PASK prefers basic residues at the P-3 and P-5 positions in substrate peptides. Our results describe the key features of the PASK structure and how those features are important for PASK activity and substrate selection.
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 structure of the kinase domain of human PASK, which provides insights into the regulatory mechanisms governing catalysis. We show that the kinase domain adopts an active conformation and has catalytic activity in vivo and in vitro in the absence of activation loop phosphorylation. Using site-directed mutagenesis and structural comparison with active and inactive kinases, we identified several key structural features in PASK that enable activation loop phosphorylation-independent activity. Finally, we used combinatorial peptide library screening to determine that PASK prefers basic residues at the P-3 and P-5 positions in substrate peptides. Our results describe the key features of the PASK structure and how those features are important for PASK activity and substrate selection.
Author Gheyi, Tarun
Iizuka, Miyo
Russell, Marijane
Zhang, Feiyu Fred
Romero, Rich
Emtage, Spencer
Rutter, Jared
Bonanno, Jeffrey B.
Antonysamy, Stephen A.
Sauder, J. Michael
Kikani, Chintan K.
Burley, Stephen K.
Turk, Benjamin E.
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  email: Rutter@biochem.utah.edu
  organization: Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, Utah 84112-5650
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Issue 52
Keywords Crystal Structure
Protein Kinases
Cell Metabolism
Protein-serine/threonine Kinase
Kinase Structure
PAS Domain
Protein Phosphorylation
PASK
Metabolism
Activation Loop Phosphorylation
Language English
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Snippet Per-Arnt-Sim (PAS) domain-containing protein kinase (PASK) is an evolutionary conserved protein kinase that coordinates cellular metabolism with metabolic...
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StartPage 41034
SubjectTerms 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
Title Structural Bases of PAS Domain-regulated Kinase (PASK) Activation in the Absence of Activation Loop Phosphorylation
URI https://dx.doi.org/10.1074/jbc.M110.157594
https://www.ncbi.nlm.nih.gov/pubmed/20943661
https://www.proquest.com/docview/820789853
https://pubmed.ncbi.nlm.nih.gov/PMC3003402
Volume 285
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