Evidence map›Paper›PMID 31604796›Full record

ArticleJournal of cell science2019

SIRT2 deacetylates GRASP55 to facilitate post-mitotic Golgi assembly.

Xiaoyan Zhang, Andreas Brachner, Eva Kukolj, Dea Slade, Yanzhuang Wang

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Golgi defect as a major contributor to lysosomal dysfunction.Frontiers in cell and developmental biology · 2024
    Review
  7. Review
  8. Review
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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

5 authors at 2 institutions in 2 countries.

Xiaoyan ZhangDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 4110 Biological Sciences Building, 1105 North University Avenue, Ann Arbor, MI 48109-1085, USA.
Andreas BrachnerDepartment of Biochemistry, Max Perutz Labs, University of Vienna, Vienna Biocenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria.
Eva KukoljDepartment of Biochemistry, Max Perutz Labs, University of Vienna, Vienna Biocenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria.
Dea SladeDepartment of Biochemistry, Max Perutz Labs, University of Vienna, Vienna Biocenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria dea.slade@univie.ac.at yzwang@umich.edu.
Yanzhuang WangDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 4110 Biological Sciences Building, 1105 North University Avenue, Ann Arbor, MI 48109-1085, USA dea.slade@univie.ac.at yzwang@umich.edu.ORCID 0000-0002-1864-7094
University of Vienna · ATUniversity of Michigan · US

Funding

Supplement: GOLGI BIOGENESIS AND FUNCTIONR35GM130331 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WANG, YANZHUANG · 2019 to 2023
$2.7M
GOLGI MATRIX ASSEMBLY AND DISASSEMBLY IN THE CELL CYCLER01GM105920 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ANDREWS, PHILIP C, WANG, YANZHUANG · 2014 to 2017
$1.9M
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
NIA NIH HHS R56 AG062225NIGMS NIH HHS R01 GM105920NIGMS NIH HHS R01 GM112786NIGMS NIH HHS R35 GM130331
6 · The paper itself

Abstract

Sirtuin 2 (SIRT2) is an NAD-dependent sirtuin deacetylase that regulates microtubule and chromatin dynamics, gene expression and cell cycle progression, as well as nuclear envelope reassembly. Recent proteomic analyses have identified Golgi proteins as SIRT2 interactors, indicating that SIRT2 may also play a role in Golgi structure formation. Here, we show that SIRT2 depletion causes Golgi fragmentation and impairs Golgi reassembly at the end of mitosis. SIRT2 interacts with the Golgi reassembly stacking protein GRASP55 (also known as GORASP2) in mitosis when GRASP55 is highly acetylated on K50. Expression of wild-type and the K50R acetylation-deficient mutant of GRASP55, but not the K50Q acetylation-mimetic mutant, in GRASP55 and GRASP65 (also known as GORASP1) double-knockout cells, rescued the Golgi structure and post-mitotic Golgi reassembly. Acetylation-deficient GRASP55 exhibited a higher self-interaction efficiency, a property required for Golgi structure formation. These results demonstrate that SIRT2 regulates Golgi structure by modulating GRASP55 acetylation levels.

Indexed as

Golgi ApparatusGolgi Matrix ProteinsHumansMicrotubulesMitosisPhosphorylationProtein Processing, Post-TranslationalSirtuin 2Golgi Matrix ProteinsGORASP2 protein, humanSIRT2 protein, humanSirtuin 2AcetylationCell cycleGolgiGolgi assemblyGRASP55SIRT2

Identifiers

PMID31604796
PMCPMC6857597
OpenAlexW2979813883

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.