Evidence map›Paper›PMID 25501367›Full record

ArticleMolecular biology of the cell2015

A unique insertion in STARD9's motor domain regulates its stability.

Silvia Senese, Keith Cheung, Yu-Chen Lo, Ankur A Gholkar, Xiaoyu Xia, James A Wohlschlegel, Jorge Z Torres

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

10 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Phospho-regulation of mitotic spindle assembly.Cytoskeleton (Hoboken, N.J.) · 2020
    Review
  4. Dissecting the mechanisms of cell division.The Journal of biological chemistry · 2019
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
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 1 institution in 1 country.

Silvia SeneseDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095.
Keith CheungDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095.
Yu-Chen LoDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095 Program in Bioengineering, University of California, Los Angeles, Los Angeles, CA 90095.
Ankur A GholkarDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095.
Xiaoyu XiaDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095.
James A WohlschlegelDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095 Jonsson Comprehensive Cancer Center, University of California, Los Angeles, Los Angeles, CA 90095 Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA 90095.
Jorge Z TorresDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095 Jonsson Comprehensive Cancer Center, University of California, Los Angeles, Los Angeles, CA 90095 Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA 90095 torres@chem.ucla.edu.
University of California, Los Angeles · US

Funding

Proteolytic Control of Iron Metabolism by the Ubiquitin Ligase FBXL5R01GM089778 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WOHLSCHLEGEL, JAMES AKIRA · 2010 to 2023
$4.0M
NIGMS NIH HHS R01 GM089778
6 · The paper itself

Abstract

STARD9 is a largely uncharacterized mitotic kinesin and putative cancer target that is critical for regulating pericentriolar material cohesion during bipolar spindle assembly. To begin to understand the mechanisms regulating STARD9 function and their importance to cell division, we took a multidisciplinary approach to define the cis and trans factors that regulate the stability of the STARD9 motor domain. We show that, unlike the other ∼50 mammalian kinesins, STARD9 contains an insertion in loop 12 of its motor domain (MD). Working with the STARD9-MD, we show that it is phosphorylated in mitosis by mitotic kinases that include Plk1. These phosphorylation events are important for targeting a pool of STARD9-MD for ubiquitination by the SCFβ-TrCP ubiquitin ligase and proteasome-dependent degradation. Of interest, overexpression of nonphosphorylatable/nondegradable STARD9-MD mutants leads to spindle assembly defects. Our results with STARD9-MD imply that in vivo the protein levels of full-length STARD9 could be regulated by Plk1 and SCFβ-TrCP to promote proper mitotic spindle assembly.

Indexed as

Amino Acid Sequencebeta-Transducin Repeat-Containing ProteinsCarrier ProteinsCell Cycle ProteinsHumansMitosisMolecular Sequence DataPhosphorylationPolo-Like Kinase 1Protein Serine-Threonine KinasesProtein Structure, TertiaryProto-Oncogene ProteinsSKP Cullin F-Box Protein LigasesSpindle ApparatusUbiquitinationbeta-Transducin Repeat-Containing ProteinsBTRC protein, humanCarrier ProteinsCell Cycle ProteinsPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsSKP Cullin F-Box Protein LigasesSTARD9 protein, human

Identifiers

PMID25501367
PMCPMC4310736
OpenAlexW2121018618

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.