Evidence map›Paper›PMID 42062288›Full record

ArticleNature communications2026

Acetylation of STX17 promotes its autophagosomal translocation.

Chenqian Zhou, Peiyang Li, Yiru Cheng, Yingchun Hu, Jingzi Wang, Xiaoyu Tian, Xun Wang, Bei Liu, Junlin Teng, Pengli Zheng and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Chenqian ZhouKey Laboratory of Cell Proliferation and Differentiation of the Ministry of Education, College of Life Sciences, Peking University, Beijing, China.
Peiyang LiNational Biomedical Imaging Center, College of Future Technology, Peking University, Beijing, China.
Yiru ChengKey Laboratory of Cell Proliferation and Differentiation of the Ministry of Education, College of Life Sciences, Peking University, Beijing, China.ORCID http://orcid.org/0009-0007-1861-6857
Yingchun HuKey Laboratory of Cell Proliferation and Differentiation of the Ministry of Education, College of Life Sciences, Peking University, Beijing, China.
Jingzi WangKey Laboratory of Cell Proliferation and Differentiation of the Ministry of Education, College of Life Sciences, Peking University, Beijing, China.
Xiaoyu TianCollaborative Innovation Center of Cell Biology in Universities of Shandong, College of Life Sciences, Shandong Normal University, Jinan, China.ORCID http://orcid.org/0000-0003-1384-8687
Xun WangState Key Laboratory of Common Mechanism Research for Major Diseases, Suzhou Institute of Systems Medicine, Chinese Academy of Medical Sciences & Peking Union Medical College, Suzhou, China.ORCID http://orcid.org/0000-0001-5172-0305
Bei LiuNational Biomedical Imaging Center, College of Future Technology, Peking University, Beijing, China. beiliu@pku.edu.cn.ORCID http://orcid.org/0000-0001-5979-3082
Junlin TengKey Laboratory of Cell Proliferation and Differentiation of the Ministry of Education, College of Life Sciences, Peking University, Beijing, China. junlinteng@pku.edu.cn.ORCID http://orcid.org/0000-0002-7611-0631
Pengli ZhengKey Laboratory of Cell Proliferation and Differentiation of the Ministry of Education, College of Life Sciences, Peking University, Beijing, China. zhengpl@pku.edu.cn.ORCID http://orcid.org/0000-0002-3797-4023
Jianguo ChenKey Laboratory of Cell Proliferation and Differentiation of the Ministry of Education, College of Life Sciences, Peking University, Beijing, China. chenjg@pku.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is a fundamental process for maintaining cell homeostasis, and STX17-mediated autophagosome-lysosome fusion is essential for cargo degradation and recycling. The translocation of STX17 to the autophagosome membrane is necessary for the fusion, yet the mechanism governing this process remains to be fully elucidated. Here, we show that following starvation, STX17 is acetylated at lysine 254 (K254), and this promotes the autophagosomal translocation of STX17 and subsequent autophagosome-lysosome fusion. Acetyltransferase GCN5 mediates STX17 K254 acetylation, which is counteracted by the deacetylase SIRT1. Moreover, autophagosomal translocation of K254-acetylated STX17 is mediated by myosin Ⅵ. Therefore, our research highlights the importance of acetylation and F-actin-based motor proteins in autophagosomal translocation of STX17 and autophagosome-lysosome fusion.

Indexed as

AutophagosomesAutophagyQa-SNARE ProteinsAcetylationActinsAnimalsHeLa CellsHumansLysineLysosomesMembrane Fusionp300-CBP-Associated FactorProtein TransportSirtuin 1ActinsLysinep300-CBP-Associated FactorQa-SNARE ProteinsSirtuin 1STX17 protein, human

Identifiers

PMID42062288
PMCPMC13338450

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.