Evidence map›Paper›PMID 20884615›Full record

ArticleThe Journal of biological chemistry2010

Cellular abundance of Mps1 and the role of its carboxyl terminal tail in substrate recruitment.

Tingting Sun, Xiaomei Yang, Wei Wang, Xiaojuan Zhang, Quanbin Xu, Songcheng Zhu, Robert Kuchta, Guanjun Chen, Xuedong Liu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

17 citing papers in PubMed, 30 citations in OpenAlex.

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  16. The MPS1 family of protein kinases.Annual review of biochemistry · 2012
    Review
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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

9 authors at 2 institutions in 2 countries.

Tingting SunDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80309, USA.
Xiaomei Yang
Wei Wang
Xiaojuan Zhang
Quanbin Xu
Songcheng Zhu
Robert Kuchta
Guanjun Chen
Xuedong Liu
University of Colorado Boulder · USShandong University · CN

Funding

Mechanisms of p27Kipl Proteolysis in Cancer CellsR01CA107098 · NCI · UNIVERSITY OF COLORADO AT BOULDER · PI LIU, XUEDONG · 2004 to 2012
$2.7M
NCI NIH HHS R01 CA107098NCI NIH HHS R01CA107098
6 · The paper itself

Abstract

Mps1 is a protein kinase that regulates normal mitotic progression and the spindle checkpoint in response to spindle damage. The levels of Mps1 are relatively low in cells during interphase but elevated in mitosis or upon activation of the spindle checkpoint, although the dynamic range of Mps1 expression and the Mps1 catalytic mechanism have not been carefully characterized. Our recent structural studies of the Mps1 kinase domain revealed that the carboxyl-terminal tail region of Mps1 is unstructured, raising the question of whether this region has any functional role in Mps1 catalysis. Here we first determined the cellular abundance of Mps1 during cell cycle progression and found that Mps1 levels vary between 60,000 per cell in early G(1) and 110,000 per cell during mitosis. We studied phosphorylation of a number of Mps1 substrates in vitro and in culture cells. Unexpectedly, we found that the unstructured carboxyl-terminal region of Mps1 plays an essential role in substrate recruitment. Kinetics studies using the purified recombinant wild type and mutant kinases indicate that the carboxyl-terminal tail is largely dispensable for autophosphorylation of Mps1 but critical for trans-phosphorylation of substrates in vitro and in cultured cells. Mps1 mutant without the unstructured tail region is defective in mediating spindle assembly checkpoint activation. Our results underscore the importance of the unstructured tail region of Mps1 in kinase activation.

Indexed as

CatalysisCell Cycle ProteinsEnzyme ActivationG1 PhaseHeLa CellsHumansMitosisMutationPhosphorylationProtein Serine-Threonine KinasesProtein Structure, TertiaryProtein-Tyrosine KinasesRecombinant ProteinsSpindle ApparatusCell Cycle ProteinsProtein Serine-Threonine KinasesProtein-Tyrosine KinasesRecombinant ProteinsTTK protein, human

Identifiers

PMID20884615
PMCPMC2992306
OpenAlexW2112299240

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.