Evidence map›Paper›PMID 24790093›Full record

ArticleMolecular biology of the cell2014

CDK-dependent phosphorylation of Alp7-Alp14 (TACC-TOG) promotes its nuclear accumulation and spindle microtubule assembly.

Naoyuki Okada, Takashi Toda, Masayuki Yamamoto, Masamitsu Sato

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

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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

4 authors at 4 institutions in 2 countries.

Naoyuki OkadaDepartment of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan.
Takashi TodaLaboratory of Cell Regulation, Cancer Research UK London Research Institute, London WC2A 3LY, United Kingdom.
Masayuki YamamotoDepartment of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Tokyo 113-0033, JapanLaboratory of Cell Response, National Institute for Basic Biology, Okazaki 444-8585, Japan.
Masamitsu SatoDepartment of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Tokyo 113-0033, JapanDepartment of Life Science and Medical Bioscience, Graduate School of Advanced Science and Engineering, Waseda University, Center for Advanced Biomedical Sciences (TWIns), Tokyo 162-8480, JapanPrecursory Research for Embryonic Science and Technology, Japan Science and Technology Agency, Kawaguchi 332-0012, Japan masasato@waseda.jp.
Cancer Research UK · GBNational Institute for Basic Biology · JPTokyo University of Science · JPWaseda University · JP

Funding

Cancer Research UK 15670
6 · The paper itself

Abstract

As cells transition from interphase to mitosis, the microtubule cytoskeleton is reorganized to form the mitotic spindle. In the closed mitosis of fission yeast, a microtubule-associated protein complex, Alp7-Alp14 (transforming acidic coiled-coil-tumor overexpressed gene), enters the nucleus upon mitotic entry and promotes spindle formation. However, how the complex is controlled to accumulate in the nucleus only during mitosis remains elusive. Here we demonstrate that Alp7-Alp14 is excluded from the nucleus during interphase using the nuclear export signal in Alp14 but is accumulated in the nucleus during mitosis through phosphorylation of Alp7 by the cyclin-dependent kinase (CDK). Five phosphorylation sites reside around the nuclear localization signal of Alp7, and the phosphodeficient alp7-5A mutant fails to accumulate in the nucleus during mitosis and exhibits partial spindle defects. Thus our results reveal one way that CDK regulates spindle assembly at mitotic entry: CDK phosphorylates the Alp7-Alp14 complex to localize it to the nucleus.

Indexed as

Active Transport, Cell NucleusAmino Acid SequenceCell NucleusCyclin-Dependent KinasesMicrotubule-Associated ProteinsMicrotubulesMolecular Sequence DataNuclear Export SignalsPhosphorylationProtein BindingProtein Processing, Post-TranslationalProtein Structure, TertiarySchizosaccharomyces pombe Proteinsalp14 protein, S pombeAlp7 protein, S pombeCyclin-Dependent KinasesMicrotubule-Associated ProteinsNuclear Export SignalsSchizosaccharomyces pombe Proteins

Identifiers

PMID24790093
PMCPMC4072571
OpenAlexW2029561563

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.