Evidence map›Paper›PMID 16275910›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Control of mammalian glycogen synthase by PAS kinase.

Wayne A Wilson, Alexander V Skurat, Brandon Probst, Anna de Paoli-Roach, Peter J Roach, Jared Rutter

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed, 51 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Glucolipotoxicity of the pancreatic beta cell.Biochimica et biophysica acta · 2010
    Review
  18. The role of PAS kinase in PASsing the glucose signal.Sensors (Basel, Switzerland) · 2010
    Review
  19. Article
  20. Article
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

6 authors at 2 institutions in 1 country.

Wayne A WilsonDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84132, USA.
Alexander V Skurat
Brandon Probst
Anna de Paoli-Roach
Peter J Roach
Jared Rutter
The University of Texas Southwestern Medical Center · USIndiana University – Purdue University Indianapolis · US

Funding

HORMONAL CONTROL OF GLYCOGEN METABOLISMR37DK027221 · NIDDK · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI ROACH, PETER J · 1992 to 2014
$5.2M
SMALL MOLECULE INHIBITION OF GLYCOGEN STORAGE AS THERAPY FOR GLYCOGENOSESR01DK027221 · NIDDK · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI HURLEY, THOMAS D. · 1986 to 2020
$4.4M
STRUCTURE &REGULATION OF TYPE 1 PROTEIN PHOSPHATASESR01DK036569 · NIDDK · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI DEPAOLI-ROACH, ANNA A · 1986 to 2004
$1.3M
SMALL MOLECULE INHIBITION OF GLYCOGEN STORAGE AS THERAPY FOR GLYCOGENOSESR56DK027221 · NIDDK · INDIANA UNIVERSITY INDIANAPOLIS · PI HURLEY, THOMAS D., ROACH, PETER J · 2015 to 2015
$185k
NIDDK NIH HHS DK27221NIDDK NIH HHS DK36569NIDDK NIH HHS R01 DK027221NIDDK NIH HHS R01 DK036569NIDDK NIH HHS R37 DK027221NIDDK NIH HHS R56 DK027221
6 · The paper itself

Abstract

The regulation of glycogen metabolism is critical for the maintenance of glucose and energy homeostasis in mammals. Glycogen synthase, the enzyme responsible for glycogen production, is regulated by multisite phosphorylation in yeast and mammals. We have previously identified PAS kinase as a physiological regulator of glycogen synthase in Saccharomyces cerevisiae. We provide evidence here that PAS kinase is an important regulator of mammalian glycogen synthase. Glycogen synthase is efficiently phosphorylated by PAS kinase in vitro at Ser-640, a known regulatory phosphosite. Efficient phosphorylation requires a region of PAS kinase outside the catalytic domain. This region appears to mediate a direct interaction between glycogen synthase and PAS kinase, thereby targeting kinase activity to this substrate specifically. This interaction is regulated by the PAS kinase PAS domain, raising the possibility that this interaction (and phosphorylation event) is modulated by the cellular metabolic state. This mode of regulation provides a mechanism for metabolic status to impinge directly on the cellular decision of whether to store or use available energy.

Indexed as

AnimalsElectrophoresis, Polyacrylamide GelGlycogenGlycogen SynthaseHistonesMammalsMusclesPhosphorylationProtein Serine-Threonine KinasesSubstrate SpecificityGlycogenGlycogen SynthaseHistonesPAS domain kinasesProtein Serine-Threonine Kinases

Identifiers

PMID16275910
PMCPMC1283851
OpenAlexW1974492531

What OpenQuestion holds

Textmetadata
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.