Evidence map›Paper›PMID 28486929›Full record

ArticleBMC cell biology2017

ULK1 phosphorylates Sec23A and mediates autophagy-induced inhibition of ER-to-Golgi traffic.

Wenjia Gan, Caiyun Zhang, Ka Yu Siu, Ayano Satoh, Julian A Tanner, Sidney Yu

Open access · goldAbstract read
In one paragraph

Article in BMC cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed, 1 pooled it
3.6field-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

34 citing papers in PubMed, 1 synthesis or guideline pooled it, 53 citations in OpenAlex.

  1. Guideline
  2. Review
  3. Article
  4. Review
  5. The AMPK Pathway: Molecular Rejuvenation of Metabolism and Mitochondria.Annual review of cell and developmental biology · 2025
    Review
  6. Review
  7. Article
  8. Physiological functions of ULK1/2.Journal of molecular biology · 2024
    Review
  9. Article
  10. NeuronalCells · 2023
    Article
  11. Article
  12. Article
  13. Sorting and Export of Proteins at the Endoplasmic Reticulum.Cold Spring Harbor perspectives in biology · 2023
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. 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 5 institutions in 3 countries.

Wenjia GanSchool of Biomedical Sciences, Shatin, N.T., Hong Kong, Special Administrative Region of China.
Caiyun ZhangSchool of Biomedical Sciences, Shatin, N.T., Hong Kong, Special Administrative Region of China.
Ka Yu SiuSchool of Biomedical Sciences, Shatin, N.T., Hong Kong, Special Administrative Region of China.
Ayano SatohThe Graduate School of Natural Science and Technology, Okayama University, Tsushima naka 3-1-1, Okayama, 7008530, Japan.
Julian A TannerSchool of Biomedical Sciences, University of Hong Kong, 21 Sassoon Road, Pok Fu Lam, Hong Kong, Special Administrative Region of China.
Sidney YuSchool of Biomedical Sciences, Shatin, N.T., Hong Kong, Special Administrative Region of China. Sidney.yu@cuhk.edu.hk.ORCID 0000-0001-9643-2729
Shatin Hospital · CNChinese University of Hong Kong · HKOkayama University · JPSun Yat-sen University · CNUniversity of Hong Kong · HK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAutophagy is an inducible autodigestive process that allows cells to recycle proteins and other materials for survival during stress and nutrient deprived conditions. The kinase ULK1 is required to activate this process. ULK1 phosphorylates a number of target proteins and regulates many cellular processes including the early secretory pathway. Recently, ULK1 has been demonstrated to phosphorylate Sec16 and affects the transport of serotonin transporter at the ER exit sites (ERES), but whether ULK1 may affect the transport of other cargo proteins and general secretion has not been fully addressed.

resultsIn this study, we identified Sec23A, a component of the COPII vesicle coat, as a target of ULK1 phosphorylation. Elevated autophagy, induced by amino acid starvation, rapamycin, or overexpression of ULK1 caused aggregation of the ERES, a region of the ER dedicated for the budding of COPII vesicles. Transport of cargo proteins was also inhibited under these conditions and was retained at the ERES. ULK1 phosphorylation of Sec23A reduced the interaction between Sec23A and Sec31A. We identified serine 207, serine 312 and threonine 405 on Sec23A as ULK1 phosphorylation sites. Among these residues, serine 207, when changed to phospho-deficient and phospho-mimicking mutants, most faithfully recapitulated the above-mentioned effects of ULK1 phospho-regulation.

conclusionThese findings identify Sec23A as a new target of ULK1 and uncover a mechanism of coordinating intracellular protein transport and autophagy.

Indexed as

AnimalsAutophagyAutophagy-Related Protein-1 HomologChlorocebus aethiopsCOP-Coated VesiclesCOS CellsEndoplasmic ReticulumGolgi ApparatusHEK293 CellsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsPhosphorylationProtein BindingProtein TransportVesicular Transport ProteinsAutophagy-Related Protein-1 HomologIntracellular Signaling Peptides and ProteinsSEC23A protein, humanSEC31A protein, humanULK1 protein, humanVesicular Transport ProteinsAutophagyCOPIIER exit sitesSec23ULK1

Identifiers

PMID28486929
PMCPMC5424413
OpenAlexW2613479431

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.