Evidence map›Paper›PMID 34876695›Full record

ArticleCommunications biology2021

Tankyrase-1-mediated degradation of Golgin45 regulates glycosyltransferase trafficking and protein glycosylation in Rab2-GTP-dependent manner.

Xihua Yue, Neeraj Tiwari, Lianhui Zhu, Hai Dang Truong Ngo, Jae-Min Lim, Bopil Gim, Shuaiyang Jing, Yijing Wang, Yi Qian, Intaek Lee

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2021. 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
1.6field-weighted citation impact, top 18% 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.

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  9. Retro-2 alters Golgi structure.Scientific reports · 2022
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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

10 authors at 3 institutions in 3 countries.

Xihua Yue *School of Life Science and Technology, ShanghaiTech University, Shanghai, China.ORCID http://orcid.org/0000-0003-3167-5660
Neeraj Tiwari *Department of Cell Biology, Yale University School of Medicine, New Haven, CT, 06520, USA.
Lianhui Zhu *School of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Hai Dang Truong NgoDepartment of Chemistry, Changwon National University, Changwon, Gyeongnam, South Korea.
Jae-Min LimDepartment of Chemistry, Changwon National University, Changwon, Gyeongnam, South Korea.
Bopil GimSchool of Physical Science and Technology, ShanghaiTech University, Shanghai, China.
Shuaiyang JingSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Yijing WangSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Yi QianSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Intaek LeeSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China. Leeintaek@ShanghaiTech.edu.cn.ORCID http://orcid.org/0000-0003-1084-674X
ShanghaiTech University · CNChangwon National University · KRYale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Altered glycosylation plays an important role during development and is also a hallmark of increased tumorigenicity and metastatic potentials of several cancers. We report here that Tankyrase-1 (TNKS1) controls protein glycosylation by Poly-ADP-ribosylation (PARylation) of a Golgi structural protein, Golgin45, at the Golgi. TNKS1 is a Golgi-localized peripheral membrane protein that plays various roles throughout the cell, ranging from telomere maintenance to Glut4 trafficking. Our study indicates that TNKS1 localization to the Golgi apparatus is mediated by Golgin45. TNKS1-dependent control of Golgin45 protein stability influences protein glycosylation, as shown by Glycomic analysis. Further, FRAP experiments indicated that Golgin45 protein level modulates Golgi glycosyltransferease trafficking in Rab2-GTP-dependent manner. Taken together, these results suggest that TNKS1-dependent regulation of Golgin45 may provide a molecular underpinning for altered glycosylation at the Golgi during development or oncogenic transformation.

Indexed as

Signal TransductionBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsGlycosylationGlycosyltransferasesHumansProtein TransportTankyrasesBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsBLZF1 protein, humanGlycosyltransferasesTankyrasesTNKS protein, human

Identifiers

PMID34876695
PMCPMC8651787
OpenAlexW4200474216

What OpenQuestion holds

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LicenceCC BY
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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.