Evidence map›Paper›PMID 29689198›Full record

ArticleDevelopmental cell2018

GRASP55 Senses Glucose Deprivation through O-GlcNAcylation to Promote Autophagosome-Lysosome Fusion.

Xiaoyan Zhang, Leibin Wang, Behnam Lak, Jie Li, Eija Jokitalo, Yanzhuang Wang

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Developmental cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed, 2 pooled it
7.6field-weighted citation impact, top 2% 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

86 citing papers in PubMed, 2 syntheses or guidelines pooled it, 168 citations in OpenAlex.

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  20. Frontiers in immunology · 2025
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26 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Xiaoyan ZhangDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 North University Avenue, Ann Arbor, MI 48109-1048, USA. Electronic address: xiaoyanz@umich.edu.
Leibin WangDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 North University Avenue, Ann Arbor, MI 48109-1048, USA.
Behnam LakCell and Molecular Biology Program, Institute of Biotechnology, University of Helsinki, P.O. Box 56, Viikinkaari 9, Helsinki 00014, Finland.
Jie LiDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 North University Avenue, Ann Arbor, MI 48109-1048, USA.
Eija JokitaloCell and Molecular Biology Program, Institute of Biotechnology, University of Helsinki, P.O. Box 56, Viikinkaari 9, Helsinki 00014, Finland.
Yanzhuang WangDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 North University Avenue, Ann Arbor, MI 48109-1048, USA; Department of Neurology, University of Michigan School of Medicine, Ann Arbor, MI 48109-1048, USA. Electronic address: yzwang@umich.edu.
University of Michigan · USUniversity of Helsinki · FI

Funding

Supplement: GOLGI BIOGENESIS AND FUNCTIONR01GM112786 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WANG, YANZHUANG · 2015 to 2019
$1.3M
Golgi-mediated Glycosylation Defects in Alzheimer’s DiseaseR56AG062225 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WANG, YANZHUANG · 2018 to 2018
$527k
NIGMS NIH HHS R01 GM112786
6 · The paper itself

Abstract

The Golgi apparatus is the central hub for protein trafficking and glycosylation in the secretory pathway. However, how the Golgi responds to glucose deprivation is so far unknown. Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions. Glucose deprivation reduces GRASP55 O-GlcNAcylation. De-O-GlcNAcylated GRASP55 forms puncta outside of the Golgi area, which co-localize with autophagosomes and late endosomes/lysosomes. GRASP55 depletion reduces autophagic flux and results in autophagosome accumulation, while expression of an O-GlcNAcylation-deficient mutant of GRASP55 accelerates autophagic flux. Biochemically, GRASP55 interacts with LC3-II on the autophagosomes and LAMP2 on late endosomes/lysosomes and functions as a bridge between LC3-II and LAMP2 for autophagosome and lysosome fusion; this function is negatively regulated by GRASP55 O-GlcNAcylation. Therefore, GRASP55 senses glucose levels through O-GlcNAcylation and acts as a tether to facilitate autophagosome maturation.

Indexed as

AcetylglucosamineAutophagosomesAutophagyEndosomesGlucoseGolgi ApparatusGolgi Matrix ProteinsHeLa CellsHumansLysosomesMembrane ProteinsProtein Processing, Post-TranslationalProtein TransportAcetylglucosamineGlucoseGolgi Matrix ProteinsGORASP2 protein, humanMembrane Proteinsautophagosome-lysosome fusionautophagyglucose starvationGolgiGolgi stacking proteinsGRASP55LAMP2LC3O-GlcNAcylationtethering

Identifiers

PMID29689198
PMCPMC8207546
OpenAlexW2799285454

What OpenQuestion holds

Textmetadata
LicenceTDM
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.