Evidence map›Paper›PMID 25825516›Full record

ArticleThe Journal of cell biology2015

A novel role of farnesylation in targeting a mitotic checkpoint protein, human Spindly, to kinetochores.

Devinderjit K Moudgil, Nathan Westcott, Jakub K Famulski, Kinjal Patel, Dawn Macdonald, Howard Hang, Gordon K T Chan

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

41 citing papers in PubMed, 66 citations in OpenAlex.

  1. Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. KNTC1 as a putative tumor oncogene in pancreatic cancer.Journal of cancer research and clinical oncology · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Cell Synchronization Techniques for Studying Mitosis.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  17. Review
  18. Article
  19. Article
  20. Phospho-regulation of mitotic spindle assembly.Cytoskeleton (Hoboken, N.J.) · 2020
    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

7 authors at 2 institutions in 2 countries.

Devinderjit K MoudgilDepartment of Oncology, University of Alberta, Edmonton, Alberta, Canada T6G 1Z2.
Nathan WestcottLaboratory of Chemical Biology and Microbial Pathogenesis, Rockefeller University, New York, NY 10065.
Jakub K FamulskiDepartment of Oncology, University of Alberta, Edmonton, Alberta, Canada T6G 1Z2.
Kinjal PatelDepartment of Oncology, University of Alberta, Edmonton, Alberta, Canada T6G 1Z2.
Dawn MacdonaldDepartment of Oncology, University of Alberta, Edmonton, Alberta, Canada T6G 1Z2.
Howard HangLaboratory of Chemical Biology and Microbial Pathogenesis, Rockefeller University, New York, NY 10065.
Gordon K T ChanDepartment of Oncology, University of Alberta, Edmonton, Alberta, Canada T6G 1Z2 gkc@ualberta.ca.
University of Alberta · CARockefeller University · US

Funding

Studies on Protein LipidationR01GM087544 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI HANG, HOWARD C · 2010 to 2023
$4.4M
NIGMS NIH HHS R01 GM087544
6 · The paper itself

Abstract

Kinetochore (KT) localization of mitotic checkpoint proteins is essential for their function during mitosis. hSpindly KT localization is dependent on the RZZ complex and hSpindly recruits the dynein-dynactin complex to KTs during mitosis, but the mechanism of hSpindly KT recruitment is unknown. Through domain-mapping studies we characterized the KT localization domain of hSpindly and discovered it undergoes farnesylation at the C-terminal cysteine residue. The N-terminal 293 residues of hSpindly are dispensable for its KT localization. Inhibition of farnesylation using a farnesyl transferase inhibitor (FTI) abrogated hSpindly KT localization without affecting RZZ complex, CENP-E, and CENP-F KT localization. We showed that hSpindly is farnesylated in vivo and farnesylation is essential for its interaction with the RZZ complex and hence KT localization. FTI treatment and hSpindly knockdown displayed the same mitotic phenotypes, indicating that hSpindly is a key FTI target in mitosis. Our data show a novel role of lipidation in targeting a checkpoint protein to KTs through protein-protein interaction.

Indexed as

Carrier ProteinsCell Cycle ProteinsCell Line, TumorChromosomal Proteins, Non-HistoneChromosome SegregationFarnesyltranstransferaseHEK293 CellsHeLa CellsHumansKinetochoresMCF-7 CellsMicrofilament ProteinsMicrotubule-Associated ProteinsM Phase Cell Cycle CheckpointsMutationProtein PrenylationCarrier ProteinsCell Cycle Proteinscentromere protein Ecentromere protein FChromosomal Proteins, Non-HistoneFarnesyltranstransferaseKNTC1 protein, humanMicrofilament ProteinsMicrotubule-Associated ProteinsRNA, Small InterferingSPDL1 protein, humanZW10 protein, human

Identifiers

PMID25825516
PMCPMC4384735
OpenAlexW2023264140

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.