Evidence map›Paper›PMID 28814501›Full record

ArticleMolecular biology of the cell2017

Knockout of the Golgi stacking proteins GRASP55 and GRASP65 impairs Golgi structure and function.

Michael E Bekier, Leibin Wang, Jie Li, Haoran Huang, Danming Tang, Xiaoyan Zhang, Yanzhuang Wang

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

64 citing papers in PubMed, 122 citations in OpenAlex.

  1. Article
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  9. A biallelic variant inLife science alliance · 2025
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  17. Review
  18. Golgi defect as a major contributor to lysosomal dysfunction.Frontiers in cell and developmental biology · 2024
    Review
  19. Article
  20. Article

4 more citing papers are in PubMed but not listed here.

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

7 authors at 1 institution in 1 country.

Michael E BekierDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048.
Leibin WangDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048.
Jie LiDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048.
Haoran HuangDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048.
Danming TangDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048.
Xiaoyan ZhangDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048.
Yanzhuang WangDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048 yzwang@umich.edu.
University of Michigan · US

Funding

Supplement: GOLGI BIOGENESIS AND FUNCTIONR01GM112786 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WANG, YANZHUANG · 2015 to 2019
$1.3M
NIGMS NIH HHS R01 GM112786
6 · The paper itself

Abstract

Golgi reassembly stacking protein of 65 kDa (GRASP65) and Golgi reassembly stacking protein of 55 kDa (GRASP55) were originally identified as Golgi stacking proteins; however, subsequent GRASP knockdown experiments yielded inconsistent results with respect to the Golgi structure, indicating a limitation of RNAi-based depletion. In this study, we have applied the recently developed clustered regularly interspaced short palindromic repeats (CRISPR)/Cas9 technology to knock out GRASP55 and GRASP65, individually or in combination, in HeLa and HEK293 cells. We show that double knockout of GRASP proteins disperses the Golgi stack into single cisternae and tubulovesicular structures, accelerates protein trafficking, and impairs accurate glycosylation of proteins and lipids. These results demonstrate a critical role for GRASPs in maintaining the stacked structure of the Golgi, which is required for accurate posttranslational modifications in the Golgi. Additionally, the GRASP knockout cell lines developed in this study will be useful tools for studying the role of GRASP proteins in other important cellular processes.

Indexed as

Base SequenceGene Knockdown TechniquesGene Knockout TechniquesGolgi ApparatusGolgi Matrix ProteinsHEK293 CellsHeLa CellsHumansIntracellular MembranesMembrane ProteinsProtein Processing, Post-TranslationalProtein TransportRNA InterferenceGolgi Matrix ProteinsGORASP1 protein, humanGORASP2 protein, humanMembrane Proteins

Identifiers

PMID28814501
PMCPMC5638586
OpenAlexW2746372947

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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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.