Evidence map›Paper›PMID 27358407›Full record

ArticleThe Journal of biological chemistry2016

Starch Binding Domain-containing Protein 1 Plays a Dominant Role in Glycogen Transport to Lysosomes in Liver.

Tao Sun, Haiqing Yi, Chunyu Yang, Priya S Kishnani, Baodong Sun

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Lysosomal glucose sensing and glycophagy in metabolism.Trends in endocrinology and metabolism: TEM · 2023
    Review
  10. Review
  11. Review
  12. Characterization of the Skeletal Muscle Proteome in Undernourished Old Rats.International journal of molecular sciences · 2022
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
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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

5 authors at 1 institution in 1 country.

Tao SunFrom the Division of Medical Genetics, Department of Pediatrics, Duke University Medical Center, Durham, North Carolina 27710.
Haiqing YiFrom the Division of Medical Genetics, Department of Pediatrics, Duke University Medical Center, Durham, North Carolina 27710.
Chunyu YangFrom the Division of Medical Genetics, Department of Pediatrics, Duke University Medical Center, Durham, North Carolina 27710.
Priya S KishnaniFrom the Division of Medical Genetics, Department of Pediatrics, Duke University Medical Center, Durham, North Carolina 27710.
Baodong SunFrom the Division of Medical Genetics, Department of Pediatrics, Duke University Medical Center, Durham, North Carolina 27710 baodong.sun@duke.edu.
Duke Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A small portion of cellular glycogen is transported to and degraded in lysosomes by acid α-glucosidase (GAA) in mammals, but it is unclear why and how glycogen is transported to the lysosomes. Stbd1 has recently been proposed to participate in glycogen trafficking to lysosomes. However, our previous study demonstrated that knockdown of Stbd1 in GAA knock-out mice did not alter lysosomal glycogen storage in skeletal muscles. To further determine whether Stbd1 participates in glycogen transport to lysosomes, we generated GAA/Stbd1 double knock-out mice. In fasted double knock-out mice, glycogen accumulation in skeletal and cardiac muscles was not affected, but glycogen content in liver was reduced by nearly 73% at 3 months of age and by 60% at 13 months as compared with GAA knock-out mice, indicating that the transport of glycogen to lysosomes was suppressed in liver by the loss of Stbd1. Exogenous expression of human Stbd1 in double knock-out mice restored the liver lysosomal glycogen content to the level of GAA knock-out mice, as did a mutant lacking the Atg8 family interacting motif (AIM) and another mutant that contains only the N-terminal 24 hydrophobic segment and the C-terminal starch binding domain (CBM20) interlinked by an HA tag. Our results demonstrate that Stbd1 plays a dominant role in glycogen transport to lysosomes in liver and that the N-terminal transmembrane region and the C-terminal CBM20 domain are critical for this function.

Indexed as

AnimalsBiological Transport, ActiveGlycogenHumansLiverLysosomesMembrane ProteinsMiceMice, KnockoutMuscle ProteinsMuscle, SkeletalMyocardiumGlycogenMembrane ProteinsMuscle Proteinsstarch-binding domain-containing protein 1, mouseSTBD1 protein, humanglycogenglycogen storage diseaseliverlysosomeStbd1transport

Identifiers

PMID27358407
PMCPMC4974364
OpenAlexW2468369126

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.