Evidence map›Paper›PMID 20810658›Full record

ArticleThe Journal of biological chemistry2010

Starch binding domain-containing protein 1/genethonin 1 is a novel participant in glycogen metabolism.

Sixin Jiang, Brigitte Heller, Vincent S Tagliabracci, Lanmin Zhai, Jose M Irimia, Anna A DePaoli-Roach, Clark D Wells, Alexander V Skurat, Peter J Roach

Erratum issuedOpen 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. An erratum has been issued. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

81 citing papers in PubMed, 143 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Autophagy in the liver.Autophagy reports · 2026
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Decoding the molecular mechanism of selective autophagy of glycogen mediated by autophagy receptor STBD1.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Lysosomal glucose sensing and glycophagy in metabolism.Trends in endocrinology and metabolism: TEM · 2023
    Review
  20. Article

21 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Sixin JiangDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA.
Brigitte Heller
Vincent S Tagliabracci
Lanmin Zhai
Jose M Irimia
Anna A DePaoli-Roach
Clark D Wells
Alexander V Skurat
Peter J Roach
Indiana University – Purdue University Indianapolis · USIndiana University School of Medicine

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
Glycogen Metabolism and Lafora DiseaseR01NS056454 · NINDS · INDIANA UNIVERSITY INDIANAPOLIS · PI ROACH, PETER J · 2009 to 2018
$3.4M
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 R01 DK027221NIDDK NIH HHS R37 DK027221NIDDK NIH HHS R56 DK027221NINDS NIH HHS NS56454NINDS NIH HHS R01 NS056454
6 · The paper itself

Abstract

Stbd1 is a protein of previously unknown function that is most prevalent in liver and muscle, the major sites for storage of the energy reserve glycogen. The protein is predicted to contain a hydrophobic N terminus and a C-terminal CBM20 glycan binding domain. Here, we show that Stbd1 binds to glycogen in vitro and that endogenous Stbd1 locates to perinuclear compartments in cultured mouse FL83B or Rat1 cells. When overexpressed in COSM9 cells, Stbd1 concentrated at enlarged perinuclear structures, co-localized with glycogen, the late endosomal/lysosomal marker LAMP1 and the autophagy protein GABARAPL1. Mutant Stbd1 lacking the N-terminal hydrophobic segment had a diffuse distribution throughout the cell. Point mutations in the CBM20 domain did not change the perinuclear localization of Stbd1, but glycogen was no longer concentrated in this compartment. Stable overexpression of glycogen synthase in Rat1WT4 cells resulted in accumulation of glycogen as massive perinuclear deposits, where a large fraction of the detectable Stbd1 co-localized. Starvation of Rat1WT4 cells for glucose resulted in dissipation of the massive glycogen stores into numerous and much smaller glycogen deposits that retained Stbd1. In vitro, in cells, and in animal models, Stbd1 consistently tracked with glycogen. We conclude that Stbd1 is involved in glycogen metabolism by binding to glycogen and anchoring it to membranes, thereby affecting its cellular localization and its intracellular trafficking to lysosomes.

Indexed as

AnimalsAutophagy-Related Protein 8 FamilyCarrier ProteinsChlorocebus aethiopsCOS CellsGlycogenIntracellular Signaling Peptides and ProteinsLysosomal-Associated Membrane Protein 1Lysosomal Membrane ProteinsMembrane ProteinsMicePoint MutationProtein Structure, TertiaryRatsAutophagy-Related Protein 8 FamilyCarrier ProteinsGabarapl2 protein, mouseGlycogenIntracellular Signaling Peptides and ProteinsLamp1 protein, mouseLamp1 protein, ratLysosomal-Associated Membrane Protein 1Lysosomal Membrane ProteinsMembrane Proteins

Identifiers

PMID20810658
PMCPMC2966110
OpenAlexW2126037064

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.