Evidence map›Paper›PMID 32344625›Full record

ReviewInternational journal of molecular sciences2020

Deubiquitinase MYSM1 in the Hematopoietic System and beyond: A Current Review.

Amanda Fiore, Yue Liang, Yun Hsiao Lin, Jacky Tung, HanChen Wang, David Langlais, Anastasia Nijnik

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  4. The roles of the ubiquitin-proteasome system in renal disease.International journal of medical sciences · 2025
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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

7 authors at 2 institutions in 1 country.

Amanda FioreDepartment of Physiology, McGill University, Montreal, QC 3655, Canada.ORCID 0000-0002-1036-1366
Yue LiangDepartment of Physiology, McGill University, Montreal, QC 3655, Canada.
Yun Hsiao LinDepartment of Physiology, McGill University, Montreal, QC 3655, Canada.ORCID 0000-0002-5035-0645
Jacky TungDepartment of Physiology, McGill University, Montreal, QC 3655, Canada.
HanChen WangDepartment of Physiology, McGill University, Montreal, QC 3655, Canada.
David LanglaisResearch Centre on Complex Traits, McGill University, Montreal, QC 3649, Canada.ORCID 0000-0003-4429-0110
Anastasia NijnikDepartment of Physiology, McGill University, Montreal, QC 3655, Canada.
McGill University · CAMcGill Genome Centre · CA

Funding

Canada Research Chairs 950-228977 X-237294CIHR Operating Grant MOP-123403CIHR Project Grant PJT-153016
6 · The paper itself

Abstract

MYSM1 has emerged as an important regulator of hematopoietic stem cell function, blood cell production, immune response, and other aspects of mammalian physiology. It is a metalloprotease family protein with deubiquitinase catalytic activity, as well as SANT and SWIRM domains. MYSM1 normally localizes to the nucleus, where it can interact with chromatin and regulate gene expression, through deubiquitination of histone H2A and non-catalytic contacts with other transcriptional regulators. A cytosolic form of MYSM1 protein was also recently described and demonstrated to regulate signal transduction pathways of innate immunity, by promoting the deubiquitination of TRAF3, TRAF6, and RIP2. In this work we review the current knowledge on the molecular mechanisms of action of MYSM1 protein in transcriptional regulation, signal transduction, and potentially other cellular processes. The functions of MYSM1 in different cell types and aspects of mammalian physiology are also reviewed, highlighting the key checkpoints in hematopoiesis, immunity, and beyond regulated by MYSM1. Importantly, mutations in MYSM1 in human were recently linked to a rare hereditary disorder characterized by leukopenia, anemia, and other hematopoietic and developmental abnormalities. Our growing knowledge of MYSM1 functions and mechanisms of actions sheds important insights into its role in mammalian physiology and the etiology of the MYSM1-deficiency disorder in human.

Indexed as

HematopoiesisAnimalsCell DifferentiationCell LineageDeubiquitinating EnzymesGene Expression RegulationHematopoietic Stem CellsHumansImmunity, InnateSignal TransductionStructure-Activity RelationshipTrans-ActivatorsUbiquitin-Specific ProteasesDeubiquitinating EnzymesMYSM1 protein, humanTrans-ActivatorsUbiquitin-Specific Proteasesdeubiquitinasehematopoiesishematopoietic stem cellsimmune responseregulation of gene expression

Identifiers

PMID32344625
PMCPMC7216186
OpenAlexW3017608774

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.