Evidence map›Paper›PMID 22167194›Full record

ArticleThe Journal of biological chemistry2012

BubR1 is modified by sumoylation during mitotic progression.

Feikun Yang, Liyan Hu, Cheng Chen, Jianxiu Yu, Christopher B O'Connell, Alexey Khodjakov, Michele Pagano, Wei Dai

RetractedErratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 26% 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, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. Mechanisms of Oocyte Maturation and Related Epigenetic Regulation.Frontiers in cell and developmental biology · 2021
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Feikun YangDepartments of Environmental Medicine and Pharmacology, New York University School of Medicine, Tuxedo, New York 10987, USA.
Liyan Hu
Cheng Chen
Jianxiu Yu
Christopher B O'Connell
Alexey Khodjakov
Michele Pagano
Wei Dai
New York University · USShanghai Jiao Tong University · CNWadsworth Center · US

Funding

REGULATION OF THE GI PHASE BY THE UBIQUITIN PATHWAYR01GM057587 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PAGANO, MICHELE · 1998 to 2018
$7.8M
FUNCTIONAL PROPERTIES OF CENTROSOMES IN SOMATIC CELLSR01GM059363 · NIGMS · WADSWORTH CENTER · PI KHODJAKOV, ALEXEY L · 1999 to 2017
$6.3M
F-box proteins: deregulated cell cycle control and proteolysis in cancerR37CA076584 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PAGANO, MICHELE · 2006 to 2016
$4.7M
Molecular mechanisms underlying chromosomal instability and aneuploidyR01CA090658 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DAI, WEI · 2001 to 2012
$2.9M
Mechanisms of arsenic-induced chromosomal instability and carcinogenesisR01ES020591 · NIEHS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DAI, WEI · 2012 to 2016
$2.0M
Novel mouse colon cancer models and chemopreventionR01CA113349 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DAI, WEI · 2006 to 2010
$1.5M
The Study of E3 Ligases and LongevityR21AG032560 · NIA · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI DILLIN, ANDREW G · 2008 to 2009
$519k
NCI NIH HHS CA090658NCI NIH HHS CA113349NCI NIH HHS R01 CA090658NCI NIH HHS R01 CA113349NCI NIH HHS R37 CA076584NIA NIH HHS R21 AG032560NIA NIH HHS R21-AG032560NIEHS NIH HHS R01 ES020591NIGMS NIH HHS R01 GM057587NIGMS NIH HHS R01-GM057587NIGMS NIH HHS R01 GM059363
6 · The paper itself

Abstract

BubR1 functions as a crucial component that monitors proper chromosome congression and mitotic timing during cell division. We investigated molecular regulation of BubR1 and found that BubR1 was modified by an unknown post-translation mechanism during the cell cycle, resulting in a significant mobility shift on denaturing gels. We termed it BubR1-M as the nature of modification was not characterized. Extended (>24 h) treatment of HeLa cells with a microtubule disrupting agent including nocodazole and taxol or release of mitotic shake-off cells into fresh medium induced BubR1-M. BubR1-M was derived from neither phosphorylation nor acetylation. Ectopic expression coupled with pulling down analyses showed that BubR1-M was derived from SUMO modification. Mutation analysis revealed that lysine 250 was a crucial site for sumoylation. Significantly, compared with the wild-type control, ectopic expression of a sumoylation-deficient mutant of BubR1 induced chromosomal missegregation and mitotic delay. Combined, our study identifies a new type of post-translational modification that is essential for BubR1 function during mitosis.

Indexed as

AcetylationAmino Acid SubstitutionHeLa CellsHumansMicrotubulesMitosisMutation, MissensePhosphorylationProtein Serine-Threonine KinasesSUMO-1 ProteinSumoylationBUB1 protein, humanBub1 spindle checkpoint proteinProtein Serine-Threonine KinasesSUMO-1 Protein

Identifiers

PMID22167194
PMCPMC3281637
OpenAlexW1983566359

What OpenQuestion holds

Textmetadata
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.