Evidence map›Paper›PMID 24048451›Full record

ArticleMolecular biology of the cell2013

SENP1 and SENP2 affect spatial and temporal control of sumoylation in mitosis.

Caelin Cubeñas-Potts, Jacqueline D Goeres, Michael J Matunis

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

36 citing papers in PubMed, 55 citations in OpenAlex.

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  5. DeSUMOylating isopeptidase 1 participates in the faithful chromosome segregation and vincristine sensitivity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
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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

3 authors at 1 institution in 1 country.

Caelin Cubeñas-PottsDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205.
Jacqueline D Goeres
Michael J Matunis
Johns Hopkins University · US

Funding

TRAINING IN AREAS FUNDAMENTAL TO CANCER RESEARCHT32CA009110 · NCI · JOHNS HOPKINS UNIVERSITY · PI MATUNIS, MICHAEL J., WEERARATNA, ASHANI T · 1985 to 2025
$13.1M
Regulation and Function of SUMO Protein Modification -Equipment SupplementR01GM060980 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI MATUNIS, MICHAEL J. · 2000 to 2023
$7.1M
NCI NIH HHS T32 CA009110NIGMS NIH HHS GM060980NIGMS NIH HHS R01 GM060980
6 · The paper itself

Abstract

Sumoylation of centromere, kinetochore, and other mitotic chromosome-associated proteins is essential for chromosome segregation. The mechanisms regulating spatial and temporal sumoylation of proteins in mitosis, however, are not well understood. Here we show that the small ubiquitin-related modifier (SUMO)-specific isopeptidases SENP1 and SENP2 are targeted to kinetochores in mitosis. SENP2 targeting occurs through a mechanism dependent on the Nup107-160 subcomplex of the nuclear pore complex and is modulated through interactions with karyopherin α. Overexpression of SENP2, but not other SUMO-specific isopeptidases, causes a defect in chromosome congression that depends on its precise kinetochore targeting. By altering SENP1 kinetochore associations, however, this effect on chromosome congression could be phenocopied. In contrast, RNA interference-mediated knockdown of SENP1 delays sister chromatid separation at metaphase, whereas SENP2 knockdown produces no detectable phenotypes. Our findings indicate that chromosome segregation depends on precise spatial and temporal control of sumoylation in mitosis and that SENP1 and SENP2 are important mediators of this control.

Indexed as

Chromosome SegregationMitosisSumoylationalpha KaryopherinsCentromereCysteine EndopeptidasesEndopeptidasesGene Expression RegulationHEK293 CellsHeLa CellsHumansKinetochoresMolecular ImagingNuclear PoreNuclear Pore Complex ProteinsNuclear Proteinsalpha KaryopherinsCysteine EndopeptidasesEndopeptidasesNuclear Pore Complex ProteinsNuclear ProteinsNUP107 protein, humanNUP160 protein, humanRNA, Small InterferingSENP1 protein, humanSENP2 protein, humanUbiquitin

Identifiers

PMID24048451
PMCPMC3826987
OpenAlexW2103558715

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.