Evidence map›Paper›PMID 34081091›Full record

ArticleThe Journal of cell biology2021

Ctf3/CENP-I provides a docking site for the desumoylase Ulp2 at the kinetochore.

Yun Quan, Stephen M Hinshaw, Pang-Che Wang, Stephen C Harrison, Huilin Zhou

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  3. Article
  4. SUMO control of centromere homeostasis.Frontiers in cell and developmental biology · 2023
    Review
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 2 institutions in 1 country.

Yun Quan *Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA.ORCID 0000-0003-3230-6189
Stephen M Hinshaw *Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Howard Hughes Medical Institute, Boston, MA.ORCID 0000-0003-4215-5206
Pang-Che WangDepartment of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA.
Stephen C HarrisonDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Howard Hughes Medical Institute, Boston, MA.ORCID 0000-0001-7215-9393
Huilin ZhouDepartment of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA.ORCID 0000-0002-1350-4430
University of California San Diego · USHoward Hughes Medical Institute · US

Funding

Suppression of duplication-mediated genome rearrangements by protein sumoylationR01GM116897 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ZHOU, HUILIN · 2015 to 2023
$2.6M
Orbitrap Fusion Mass SpectrometerS10OD023498 · OD · LUDWIG INSTITUTE FOR CANCER RES LTD · PI ZHOU, HUILIN · 2017 to 2017
$600k
NIGMS NIH HHS R01 GM116897NIH HHS S10 OD023498
6 · The paper itself

Abstract

The step-by-step process of chromosome segregation defines the stages of the cell cycle. In eukaryotes, signals controlling these steps converge upon the kinetochore, a multiprotein assembly that connects spindle microtubules to chromosomal centromeres. Kinetochores control and adapt to major chromosomal transactions, including replication of centromeric DNA, biorientation of sister centromeres on the metaphase spindle, and transit of sister chromatids into daughter cells during anaphase. Although the mechanisms that ensure tight microtubule coupling at anaphase are at least partly understood, kinetochore adaptations that support other cell cycle transitions are not. We report here a mechanism that enables regulated control of kinetochore sumoylation. A conserved surface of the Ctf3/CENP-I kinetochore protein provides a binding site for Ulp2, the nuclear enzyme that removes SUMO chains from modified substrates. Ctf3 mutations that disable Ulp2 recruitment cause elevated inner kinetochore sumoylation and defective chromosome segregation. The location of the site within the assembled kinetochore suggests coordination between sumoylation and other cell cycle-regulated processes.

Indexed as

Chromosome SegregationChromosomes, FungalCryoelectron MicroscopyEndopeptidasesKinetochoresMicroscopy, FluorescenceModels, MolecularMutationProtein BindingProtein Interaction Domains and MotifsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSumoylationCtf3 protein, S cerevisiaeEndopeptidasesSaccharomyces cerevisiae ProteinsULP2 protein, S cerevisiae

Identifiers

PMID34081091
PMCPMC8178754
OpenAlexW3164161752

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.