Evidence map›Paper›PMID 24196834›Full record

ArticleMolecular biology of the cell2014

The SUMO proteases SENP1 and SENP2 play a critical role in nucleoporin homeostasis and nuclear pore complex function.

Kin-Hoe Chow, Suzanne Elgort, Mary Dasso, Maureen A Powers, Katharine S Ullman

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

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  16. SUMO protease SENP1 deSUMOylates and stabilizes c-Myc.Proceedings of the National Academy of Sciences of the United States of America · 2018
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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 3 institutions in 1 country.

Kin-Hoe ChowDepartment of Oncological Sciences, Huntsman Cancer Institute, University of Utah, Salt Lake City, UT 84112 Laboratory of Gene Regulation and Development, National Institute for Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892 Department of Cell Biology, Emory University School of Medicine, Atlanta, GA 30322.
Suzanne Elgort
Mary Dasso
Maureen A Powers
Katharine S Ullman
University of Utah · USEmory University · USNational Institutes of Health · US

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 1986 to 2026
$72.6M
SUMO family Ubiquitin-like Modifiers In Higher EukaryotesZIAHD001902 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI DASSO, MARY C. · 2009 to 2021
$6.3M
The Nuclear Pore Complex: Interphase and Mitotic FunctionR01GM061275 · NIGMS · UNIVERSITY OF UTAH · PI ULLMAN, KATHARINE S · 2000 to 2012
$3.6M
Mitotic roles of Nuclear Pore Complex (NPC) proteinsZIAHD008816 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI DASSO, MARY C. · 2009 to 2014
$3.3M
FUNCTIONAL ANALYSIS OF VERTEBRATE NUCLEAR TRANSPORTR01GM059975 · NIGMS · EMORY UNIVERSITY · PI POWERS, MAUREEN A. · 1999 to 2009
$2.4M
The Small Ubiquitin-like Modifier Sumo-1 In Higher EukarZ01HD001902 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI DASSO, MARY C. · 1995 to 2008
$1.3M
Mitotic roles of Nuclear Pore Complex (NPC) proteinsZ01HD008816 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI DASSO, MARY C. · 2007 to 2008
$762k
Intramural NIH HHS Z01 HD001902Intramural NIH HHS Z01 HD008816NCI NIH HHS P30 CA042014NIGMS NIH HHS R01 GM059975NIGMS NIH HHS R01 GM061275NIGMS NIH HHS R01 GM61275
6 · The paper itself

Abstract

Nuclear pore complexes are composed of ∼30 different proteins, each present at the pore in multiple copies. Together these proteins create specialized channels that convey cargo between the cytoplasm and the nuclear interior. With the building blocks of nuclear pores identified, one challenge is to decipher how these proteins are coordinately produced and assembled into macromolecular pore structures with each cell division. Specific individual pore proteins and protein cofactors have been probed for their role in the assembly process, as well as certain kinases that add a layer of regulation via the phosphorylation status of nucleoporins. Other posttranslational modifications are candidates for coordinating events of pore assembly as well. In this study of two pore-associated small ubiquitin-like modifier (SUMO) proteases, sentrin/SUMO-specific protease 1 (SENP1) and SENP2, we observe that many nucleoporins are mislocalized and, in some cases, reduced in level when SENP1 and SENP2 are codepleted. The pore complexes present under these conditions are still capable of transport, although the kinetics of specific cargo is altered. These results reveal a new role for the pore-associated SENPs in nucleoporin homeostasis and in achieving proper configuration of the nuclear pore complex.

Indexed as

HomeostasisActive Transport, Cell NucleusCysteine EndopeptidasesEndopeptidasesGene Knockdown TechniquesHeLa CellsHumansInterphaseMembrane GlycoproteinsMembrane ProteinsMicrotubule-Associated ProteinsNuclear PoreNuclear Pore Complex ProteinsNuclear ProteinsRNA, Small InterferingCysteine EndopeptidasesEndopeptidasesMembrane GlycoproteinsMembrane ProteinsMicrotubule-Associated ProteinsNuclear Pore Complex ProteinsNuclear ProteinsPOM121 protein, humanRNA, Small InterferingSENP1 protein, humanSENP2 protein, humanSUN1 protein, human

Identifiers

PMID24196834
PMCPMC3873886
OpenAlexW2147030635

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.