Evidence map›Paper›PMID 20943661›Full record

ArticleThe Journal of biological chemistry2010

Structural bases of PAS domain-regulated kinase (PASK) activation in the absence of activation loop phosphorylation.

Chintan K Kikani, Stephen A Antonysamy, Jeffrey B Bonanno, Rich Romero, Feiyu Fred Zhang, Marijane Russell, Tarun Gheyi, Miyo Iizuka, Spencer Emtage, J Michael Sauder and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.4field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Structural assembly of the PAS domain drives the catalytic activation of metazoan PASK.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
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  9. Activation of PASK by mTORC1 is required for the onset of the terminal differentiation program.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
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  14. Review
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  18. Review
  19. Article
  20. PAS kinase: integrating nutrient sensing with nutrient partitioning.Seminars in cell & developmental biology · 2012
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 5 institutions in 1 country.

Chintan K KikaniDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, Utah 84112-5650, USA.
Stephen A Antonysamy
Jeffrey B Bonanno
Rich Romero
Feiyu Fred Zhang
Marijane Russell
Tarun Gheyi
Miyo Iizuka
Spencer Emtage
J Michael Sauder
Benjamin E Turk
Stephen K Burley
Jared Rutter
Eli Lilly (United States) · USCox & Company (United States) · USUniversity of Utah · USAlbert Einstein College of Medicine · USYale University · US

Funding

SUBPROJECT 5U54GM074945 · NIGMS · SGX PHARMACEUTICALS, INC. · PI BURLEY, STEPHEN KEVIN · 2005 to 2009
$46.2M
The role of PAS kinase in hepatic lipid metabolismR01DK071962 · NIDDK · UNIVERSITY OF UTAH · PI RUTTER, JARED P · 2005 to 2013
$2.4M
Proteome-wide analysis of kinase phosphorylation specificity in yeastR01GM079498 · NIGMS · YALE UNIVERSITY · PI TURK, BENJAMIN E · 2007 to 2011
$1.8M
The role of PAS kinase in hepatic lipid metabolismR56DK071962 · NIDDK · UNIVERSITY OF UTAH · PI RUTTER, JARED P · 2009 to 2009
$376k
NIDDK NIH HHS DK071962NIDDK NIH HHS R01 DK071962NIDDK NIH HHS R56 DK071962NIGMS NIH HHS GM079498NIGMS NIH HHS R01 GM079498NIGMS NIH HHS U54 GM074945
6 · The paper itself

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.

Indexed as

Enzyme ActivationHumansMutagenesis, Site-DirectedPhosphorylationProtein Serine-Threonine KinasesProtein Structure, SecondaryProtein Structure, TertiaryStructure-Activity RelationshipPAS domain kinasesProtein Serine-Threonine Kinases

Identifiers

PMID20943661
PMCPMC3003402
OpenAlexW2016229856

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.