Evidence map›Paper›PMID 28695742›Full record

ArticleJournal of proteome research2017

Human Regulatory Protein Ki-1/57 Is a Target of SUMOylation and Affects PML Nuclear Body Formation.

Ângela Saito, Edmarcia E Souza, Fernanda C Costa, Gabriela V Meirelles, Kaliandra A Gonçalves, Marcos T Santos, Gustavo C Bressan, Mark E McComb, Catherine E Costello, Stephen A Whelan and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of proteome research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

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  5. Mechanistic update of Trisenox in blood cancer.Current research in pharmacology and drug discovery · 2023
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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

11 authors at 5 institutions in 2 countries.

Ângela SaitoLaboratório Nacional de Biociências (LNBio), Centro Nacional de Pesquisa em Energia e Materiais (CNPEM) , Campinas, São Paulo 13083-970, Brazil.
Edmarcia E SouzaFaculdade de Ciências Farmacêuticas, Universidade Estadual de Campinas , Campinas, São Paulo 13083-859, Brazil.
Fernanda C CostaInstituto de Física de São Carlos, Universidade de São Paulo , São Carlos, São Paulo 13563-120, Brazil.
Gabriela V MeirellesLaboratório Nacional de Biociências (LNBio), Centro Nacional de Pesquisa em Energia e Materiais (CNPEM) , Campinas, São Paulo 13083-970, Brazil.
Kaliandra A GonçalvesLaboratório Nacional de Biociências (LNBio), Centro Nacional de Pesquisa em Energia e Materiais (CNPEM) , Campinas, São Paulo 13083-970, Brazil.
Marcos T SantosONKOS Molecular Diagnostics, Inc. , R&D Department, Ribeirão Preto, São Paulo 14056-680, Brazil.
Gustavo C BressanDepartamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa (UFV) , Viçosa, Minas Gerais 36570-000, Brazil.
Mark E McCombCenter for Biomedical Mass Spectrometry, Boston University School of Medicine , Boston, Massachusetts 02118, United States.
Catherine E CostelloCenter for Biomedical Mass Spectrometry, Boston University School of Medicine , Boston, Massachusetts 02118, United States.ORCID 0000-0003-1594-5122
Stephen A WhelanCenter for Biomedical Mass Spectrometry, Boston University School of Medicine , Boston, Massachusetts 02118, United States.
Jörg KobargFaculdade de Ciências Farmacêuticas, Universidade Estadual de Campinas , Campinas, São Paulo 13083-859, Brazil.ORCID 0000-0002-9419-0145
Boston University · USLaboratório Nacional de Ciência e Tecnologia do Bioetanol · BRUniversidade Estadual de Campinas (UNICAMP) · BRUniversidade Federal de São Carlos · BRUniversidade Federal de Viçosa · BR

Funding

Mass Spectrometry Resource for Biology and MedicineP41GM104603 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2012 to 2017
$10.4M
NHLBI PROTEOMICS INITIATIVE-N01HV28178N01HV028178 · HV · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2002 to 2006
–
NHLBI NIH HHS HHSN268201000031CNHLBI NIH HHS N01 HV028178NIGMS NIH HHS P41 GM104603
6 · The paper itself

Abstract

Ki-1/57 is a nuclear and cytoplasmic regulatory protein first identified in malignant cells from Hodgkin's lymphoma. It is involved in gene expression regulation on both transcriptional and mRNA metabolism levels. Ki-1/57 belongs to the family of intrinsically unstructured proteins and undergoes phosphorylation by PKC and methylation by PRMT1. Previous characterization of its protein interaction profile by yeast two-hybrid screening showed that Ki-1/57 interacts with proteins of the SUMOylation machinery, the SUMO E2 conjugating enzyme UBC9 and the SUMO E3 ligase PIAS3, which suggested that Ki-1/57 could be involved with this process. Here we identified seven potential SUMO target sites (lysine residues) on Ki-1/57 sequence and observed that Ki-1/57 is modified by SUMO proteins in vitro and in vivo. We showed that SUMOylation of Ki-1/57 occurred on lysines 213, 276, and 336. In transfected cells expressing FLAG-Ki-1/57 wild-type, its paralog FLAG-CGI-55 wild-type, or their non-SUMOylated triple mutants, the number of PML-nuclear bodies (PML-NBs) is reduced compared with the control cells not expressing the constructs. More interestingly, after treating cells with arsenic trioxide (As

Indexed as

Protein Interaction MappingProtein Processing, Post-TranslationalArsenicalsArsenic TrioxideCell CycleCell NucleusCloning, MolecularEscherichia coliHEK293 CellsHeLa CellsHumansLysineMyogenic Regulatory FactorsOligopeptidesOxidesPlasmidsArsenicalsArsenic TrioxideFLAG peptideHABP4 protein, humanLysineMyogenic Regulatory FactorsOligopeptidesOxidesRecombinant Fusion ProteinsRNA-Binding ProteinsSERBP1 protein, humanSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSUMO1 protein, humanSUMO2 protein, humanarsenic trioxideCGI-55Ki-1/57PML-NBsposttranslational modificationsSUMOylation

Identifiers

PMID28695742
PMCPMC6699623
OpenAlexW2736301858

What OpenQuestion holds

Textmetadata
LicenceTDM
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.