Evidence map›Paper›PMID 31434716›Full record

ArticleJournal of cell science2019

Phosphorylation of importin-α1 by CDK1-cyclin B1 controls mitotic spindle assembly.

Li Guo, Khamsah Suryati Mohd, He Ren, Guangwei Xin, Qing Jiang, Paul R Clarke, Chuanmao Zhang

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

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  14. Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022
    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

7 authors at 3 institutions in 3 countries.

Li GuoThe MOE Key Laboratory of Cell Proliferation and Differentiation, College of Life Sciences, Peking University, Beijing 100871, China.
Khamsah Suryati MohdSchool of Medicine, Jacqui Wood Cancer Centre, Ninewells Hospital and Medical School, University of Dundee, Dundee DD1 9SY, UK.
He RenThe MOE Key Laboratory of Cell Proliferation and Differentiation, College of Life Sciences, Peking University, Beijing 100871, China.
Guangwei XinThe MOE Key Laboratory of Cell Proliferation and Differentiation, College of Life Sciences, Peking University, Beijing 100871, China.
Qing JiangThe MOE Key Laboratory of Cell Proliferation and Differentiation, College of Life Sciences, Peking University, Beijing 100871, China.
Paul R ClarkeSchool of Medicine, Jacqui Wood Cancer Centre, Ninewells Hospital and Medical School, University of Dundee, Dundee DD1 9SY, UK paul.clarke@uq.edu.au zhangcm@pku.edu.cn.ORCID 0000-0003-3525-2622
Chuanmao ZhangThe MOE Key Laboratory of Cell Proliferation and Differentiation, College of Life Sciences, Peking University, Beijing 100871, China paul.clarke@uq.edu.au zhangcm@pku.edu.cn.
Peking University · CNThe University of Queensland · AUUniversity of Dundee · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G001480/1Cancer Research UK 13424
6 · The paper itself

Abstract

Importin-α serves as an adaptor linking importin-β to proteins carrying a nuclear localization sequence (NLS). During interphase, this interaction enables nuclear protein import, while in mitosis it regulates spindle assembly factors (SAFs) and controls microtubule nucleation, stabilization and spindle function. Here, we show that human importin-α1 is regulated during the cell cycle and is phosphorylated at two sites (threonine 9 and serine 62) during mitosis by the major mitotic protein kinase CDK1-cyclin B. Mutational analysis indicates that the mitotic phosphorylation of importin-α1 inhibits its binding to importin-β and promotes the release of TPX2 and KIFC1, which are then targeted like importin-β to the spindle. Loss of importin-α1 or expression of a non-phosphorylated mutant of importin-α1 results in the formation of shortened spindles with reduced microtubule density and induces a prolonged metaphase, whereas phosphorylation-mimicking mutants are functional in mitosis. We propose that phosphorylation of importin-α1 is a general mechanism for the spatial and temporal control of mitotic spindle assembly by CDK1-cyclin B1 that acts through the release of SAFs such as TPX2 and KIFC1 from inhibitory complexes that restrict spindle assembly.

Indexed as

alpha Karyopherinsbeta KaryopherinsCDC2 Protein KinaseCell Cycle ProteinsCyclin B1Electrophoresis, Polyacrylamide GelHeLa CellsHumansImmunoprecipitationMicrotubulesMitosisPhosphorylationSpindle Apparatusalpha Karyopherinsbeta KaryopherinsCDC2 Protein KinaseCell Cycle ProteinsCyclin B1Cell cycleCyclin-dependent kinaseImportinMitosisSpindle assembly

Identifiers

PMID31434716
PMCPMC6765185
OpenAlexW2969920562

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.