Evidence map›Paper›PMID 19015317›Full record

ArticleThe Journal of cell biology2008

Phosphorylation sites in BubR1 that regulate kinetochore attachment, tension, and mitotic exit.

Haomin Huang, James Hittle, Francesca Zappacosta, Roland S Annan, Avram Hershko, Timothy J Yen

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

55 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Phospho-regulation of mitotic spindle assembly.Cytoskeleton (Hoboken, N.J.) · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Protein phosphatases in the regulation of mitosis.The Journal of cell biology · 2019
    Review
  17. Article
  18. Kinase and Phosphatase Cross-Talk at the Kinetochore.Frontiers in cell and developmental biology · 2018
    Review
  19. Review
  20. 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

6 authors at 3 institutions in 2 countries.

Haomin HuangFox Chase Cancer Center, Philadelphia, PA 19111, USA.
James Hittle
Francesca Zappacosta
Roland S Annan
Avram Hershko
Timothy J Yen
Fox Chase Cancer Center · USGlaxoSmithKline (United States) · USTechnion – Israel Institute of Technology · IL

Funding

WORD PROCESSING CENTER--COREP30CA006927 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI Margaret von Mehren · 1985 to 2026
$138.8M
KINETOCHORE STRUCTURE/FUNCTIONR01GM044762 · NIGMS · RESEARCH INST OF FOX CHASE CAN CTR · PI YEN, TIMOTHY · 1992 to 2010
$2.4M
Mechanism of Mitotic Checkpoint in Mammalian CellsR01GM086877 · NIGMS · RESEARCH INST OF FOX CHASE CAN CTR · PI YEN, TIMOTHY · 2008 to 2011
$1.6M
NCI NIH HHS CA06927NCI NIH HHS P30 CA006927NIGMS NIH HHS GM44762NIGMS NIH HHS GM86877NIGMS NIH HHS R01 GM044762NIGMS NIH HHS R01 GM086877
6 · The paper itself

Abstract

BubR1 kinase is essential for the mitotic checkpoint and also for kinetochores to establish microtubule attachments. In this study, we report that BubR1 is phosphorylated in mitosis on four residues that differ from sites recently reported to be phosphorylated by Plk1 (Elowe, S., S. Hummer, A. Uldschmid, X. Li, and E.A. Nigg. 2007. Genes Dev. 21:2205-2219; Matsumura, S., F. Toyoshima, and E. Nishida. 2007. J. Biol. Chem. 282:15217-15227). S670, the most conserved residue, is phosphorylated at kinetochores at the onset of mitosis and dephosphorylated before anaphase onset. Unlike the Plk1-dependent S676 phosphorylation, S670 phosphorylation is sensitive to microtubule attachments but not to kinetochore tension. Functionally, phosphorylation of S670 is essential for error correction and for kinetochores with end-on attachments to establish tension. Furthermore, in vitro data suggest that the phosphorylation status of BubR1 is important for checkpoint inhibition of the anaphase-promoting complex/cyclosome. Finally, RNA interference experiments show that Mps1 is a major but not the exclusive kinase that specifies BubR1 phosphorylation in vivo. The combined data suggest that BubR1 may be an effector of multiple kinases that are involved in discrete aspects of kinetochore attachments and checkpoint regulation.

Indexed as

AnaphaseAnaphase-Promoting Complex-CyclosomeCell Cycle ProteinsHeLa CellsHumansKinetochoresMicrotubulesPhosphorylationProtein Serine-Threonine KinasesProtein-Tyrosine KinasesRNA, Small InterferingUbiquitin-Protein Ligase ComplexesAnaphase-Promoting Complex-CyclosomeBUB1 protein, humanBub1 spindle checkpoint proteinCell Cycle ProteinsProtein Serine-Threonine KinasesProtein-Tyrosine KinasesRNA, Small InterferingTTK protein, humanUbiquitin-Protein Ligase Complexes

Identifiers

PMID19015317
PMCPMC2582891
OpenAlexW2050321764

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.