Evidence map›Paper›PMID 33044554›Full record

ArticleThe Journal of cell biology2020

The mitotic protein NuMA plays a spindle-independent role in nuclear formation and mechanics.

Andrea Serra-Marques, Ronja Houtekamer, Dorine Hintzen, John T Canty, Ahmet Yildiz, Sophie Dumont

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-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

17 citing papers in PubMed, 24 citations in OpenAlex.

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  13. Mechanics and functional consequences of nuclear deformations.Nature reviews. Molecular cell biology · 2022
    Review
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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

6 authors at 2 institutions in 1 country.

Andrea Serra-MarquesDepartment of Cell and Tissue Biology, University of California, San Francisco, San Francisco, CA.
Ronja HoutekamerDepartment of Cell and Tissue Biology, University of California, San Francisco, San Francisco, CA.
Dorine HintzenDepartment of Cell and Tissue Biology, University of California, San Francisco, San Francisco, CA.
John T CantyBiophysics Graduate Group, University of California, Berkeley, Berkeley, CA.
Ahmet YildizBiophysics Graduate Group, University of California, Berkeley, Berkeley, CA.
Sophie DumontDepartment of Cell and Tissue Biology, University of California, San Francisco, San Francisco, CA.
University of California, San Francisco · USUniversity of California, Berkeley · US

Funding

Research BaseP30DK063720 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GERMAN, MICHAEL S · 2003 to 2019
$21.8M
MOLECULAR BIOPHYSICS TRAINING GRANTT32GM008295 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HURLEY, JAMES H, WEMMER, DAVID E · 1989 to 2022
$8.1M
Assembly and function of cytoskeletal systems in eukaryotic and prokaryoticcellsR35GM118119 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MULLINS, R DYCHE · 2016 to 2025
$4.8M
Microscopy system upgradeR35GM136420 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Sophie Dumont · 2020 to 2026
$4.6M
Rewiring cellular architecture to probe mechanical signal processing at kinetochoresDP2GM119177 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DUMONT, SOPHIE · 2015 to 2015
$2.4M
BD FACSAria Fusion Cell SorterS10OD021822 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI LEE, MICHAEL R. · 2016 to 2016
$573k
Mechanics of the dynamic mammalian kinetochore-microtubule interfaceR01GM134132 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DUMONT, SOPHIE · 2019 to 2019
$364k
Howard Hughes Medical InstituteNIDDK NIH HHS P30 DK063720NIGMS NIH HHS DP2 GM119177NIGMS NIH HHS R01 GM134132NIGMS NIH HHS R35 GM118119NIGMS NIH HHS R35 GM136420NIGMS NIH HHS T32 GM008295NIH HHS S10 OD021822
6 · The paper itself

Abstract

Eukaryotic cells typically form a single, round nucleus after mitosis, and failures to do so can compromise genomic integrity. How mammalian cells form such a nucleus remains incompletely understood. NuMA is a spindle protein whose disruption results in nuclear fragmentation. What role NuMA plays in nuclear integrity, and whether its perceived role stems from its spindle function, are unclear. Here, we use live imaging to demonstrate that NuMA plays a spindle-independent role in forming a single, round nucleus. NuMA keeps the decondensing chromosome mass compact at mitotic exit and promotes a mechanically robust nucleus. NuMA's C terminus binds DNA in vitro and chromosomes in interphase, while its coiled-coil acts as a central regulatory and structural element: it prevents NuMA from binding chromosomes at mitosis, regulates its nuclear mobility, and is essential for nuclear formation. Thus, NuMA plays a structural role over the cell cycle, building and maintaining the spindle and nucleus, two of the cell's largest structures.

Indexed as

MitosisCell Cycle ProteinsCell NucleusChromosomes, HumanDNAHEK293 CellsHumansInterphaseSpindle ApparatusCell Cycle ProteinsDNANUMA1 protein, human

Identifiers

PMID33044554
PMCPMC7555356
OpenAlexW3092151253

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.