Evidence map›Paper›PMID 31239341›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Atlastin-mediated membrane tethering is critical for cargo mobility and exit from the endoplasmic reticulum.

Liling Niu, Tianji Ma, Feng Yang, Bing Yan, Xiao Tang, Haidi Yin, Qian Wu, Yan Huang, Zhong-Ping Yao, Jifeng Wang and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

35 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
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  3. A class of COPI cargo receptors regulates processing of transmembrane proteins by reinforcing their Golgi retention.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  11. TMED10 mediates the trafficking of insulin-like growth factor 2 along the secretory pathway for myoblast differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  16. Review
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  20. A role for endoplasmic reticulum dynamics in the cellular distribution of microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

12 authors at 3 institutions in 2 countries.

Liling NiuNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101 Beijing, China.
Tianji MaDivision of Life Science, Hong Kong University of Science and Technology, Hong Kong, China.
Feng YangDivision of Life Science, Hong Kong University of Science and Technology, Hong Kong, China.
Bing YanNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101 Beijing, China.
Xiao TangDivision of Life Science, Hong Kong University of Science and Technology, Hong Kong, China.
Haidi YinState Key Laboratory of Chemical Biology and Drug Discovery, Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hong Kong, China.
Qian WuState Key Laboratory of Chemical Biology and Drug Discovery, Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hong Kong, China.
Yan HuangDivision of Life Science, Hong Kong University of Science and Technology, Hong Kong, China.
Zhong-Ping YaoState Key Laboratory of Chemical Biology and Drug Discovery, Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hong Kong, China.ORCID 0000-0003-3555-9632
Jifeng WangNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101 Beijing, China.
Yusong GuoDivision of Life Science, Hong Kong University of Science and Technology, Hong Kong, China; guoyusong@ust.hk huj@ibp.ac.cn.
Junjie HuNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101 Beijing, China; guoyusong@ust.hk huj@ibp.ac.cn.ORCID 0000-0003-4712-2243
Hong Kong University of Science and Technology · HKChinese Academy of Sciences · CNHong Kong Polytechnic University · HK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endoplasmic reticulum (ER) membrane junctions are formed by the dynamin-like GTPase atlastin (ATL). Deletion of ATL results in long unbranched ER tubules in cells, and mutation of human ATL1 is linked to hereditary spastic paraplegia. Here, we demonstrate that COPII formation is drastically decreased in the periphery of ATL-deleted cells. ER export of cargo proteins becomes defective; ER exit site initiation is not affected, but many of the sites fail to recruit COPII subunits. The efficiency of cargo packaging into COPII vesicles is significantly reduced in cells lacking ATLs, or when the ER is transiently fragmented. Cargo is less mobile in the ER in the absence of ATL, but the cargo mobility and COPII formation can be restored by ATL R77A, which is capable of tethering, but not fusing, ER tubules. These findings suggest that the generation of ER junctions by ATL plays a critical role in maintaining the necessary mobility of ER contents to allow efficient packaging of cargo proteins into COPII vesicles.

Indexed as

AnimalsChlorocebus aethiopsCOP-Coated VesiclesCOS CellsEndoplasmic ReticulumGolgi ApparatusGTP-Binding ProteinsHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMutant ProteinsProtein TransportSequence DeletionSpastic Paraplegia, HereditaryATL1 protein, humanGTP-Binding ProteinsIntracellular Signaling Peptides and ProteinsMembrane ProteinsMutant ProteinsVANGL2 protein, humanatlastinCOPII formationendoplasmic reticulummembrane tensionprotein mobility

Identifiers

PMID31239341
PMCPMC6628656
OpenAlexW2955671834

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.