Evidence map›Paper›PMID 26363069›Full record

ArticleThe Journal of biological chemistry2015

Structural basis for the interaction between the Golgi reassembly-stacking protein GRASP65 and the Golgi matrix protein GM130.

Fen Hu, Xiaoli Shi, Bowen Li, Xiaochen Huang, Xavier Morelli, Ning Shi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Golgi defect as a major contributor to lysosomal dysfunction.Frontiers in cell and developmental biology · 2024
    Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. New Insights Into the Golgi Stacking Proteins.Frontiers in cell and developmental biology · 2019
    Review
  14. Golgi Structure and Function in Health, Stress, and Diseases.Results and problems in cell differentiation · 2019
    Review
  15. Article
  16. Article
  17. Review
  18. Glycosylation Quality Control by the Golgi Structure.Journal of molecular biology · 2016
    Review
  19. Article
  20. GRASP: A Multitasking Tether.Frontiers in cell and developmental biology · 2016
    Review
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 3 institutions in 2 countries.

Fen HuFrom the State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou 350002, China and.
Xiaoli ShiFrom the State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou 350002, China and.
Bowen LiFrom the State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou 350002, China and.
Xiaochen HuangFrom the State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou 350002, China and.
Xavier Morellithe CNRS UMR7258, INSERM U1068, Aix-Marseille Université UM105, Institut Paoli-Calmettes, Marseille F-13009, France.
Ning ShiFrom the State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou 350002, China and shining@fjirsm.ac.cn ningshi2000@hotmail.com.
Fujian Institute of Research on the Structure of Matter · CNChinese Academy of Sciences · CNInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

GM130 and GRASP65 are Golgi peripheral membrane proteins that play a key role in Golgi stacking and vesicle tethering. However, the molecular details of their interaction and their structural role as a functional unit remain unclear. Here, we present the crystal structure of the PDZ domains of GRASP65 in complex with the GM130 C-terminal peptide at 1.96-Å resolution. In contrast to previous findings proposing that GM130 interacts with GRASP65 at the PDZ2 domain only, our crystal structure of the complex indicates that GM130 binds to GRASP65 at two distinct sites concurrently and that both the PDZ1 and PDZ2 domains of GRASP65 participate in this molecular interaction. Mutagenesis experiments support these structural observations and demonstrate that they are required for GRASP65-GM130 association.

Indexed as

AutoantigensCrystallography, X-RayGolgi ApparatusGolgi Matrix ProteinsHeLa CellsHumansMembrane ProteinsMutagenesisPDZ DomainsProtein Structure, QuaternaryAutoantigensGolgi Matrix ProteinsGolgin subfamily A member 2GORASP1 protein, humanMembrane ProteinsGM130, GRASP65, PDZ domain, Golgi stacking, vesicle tetheringGolgiprotein assemblyprotein complexprotein-protein interactionvesicles

Identifiers

PMID26363069
PMCPMC4646294
OpenAlexW2191697503

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.