Evidence map›Paper›PMID 9679058›Full record

ArticleGenes & development1998

Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1.

J Yang, E S Bardes, J D Moore, J Brennan, M A Powers, S Kornbluth

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.

0numbers the graph read from it
0cells of the map it votes in
137citing papers in PubMed
–field-weighted citation impact
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

137 citing papers in PubMed, 319 citations in OpenAlex.

  1. Article
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  11. DNA damage checkpoint execution and the rules of its disengagement.Frontiers in cell and developmental biology · 2022
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77 more citing papers are in PubMed but not listed here.

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

6 authors at 4 institutions in 1 country.

J YangDepartment of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710 USA.
E S Bardes
J D Moore
J Brennan
M A Powers
S Kornbluth
Duke University · USEmory University · USDuke Medical Center · USDuke University Hospital · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activation of the Cyclin B/Cdc2 kinase complex triggers entry into mitosis in all eukaryotic cells. Cyclin B1 localization changes dramatically during the cell cycle, precipitously transiting from the cytoplasm to the nucleus at the beginning of mitosis. Presumably, this relocalization promotes the phosphorylation of nuclear targets critical for chromatin condensation and nuclear envelope breakdown. We show here that the previously characterized cytoplasmic retention sequence of Cyclin B1, responsible for its interphase cytoplasmic localization, is actually an autonomous nuclear export sequence, capable of directing nuclear export of a heterologous protein, and able to bind specifically to the recently identified export mediator, CRM1. We propose that the observed cytoplasmic localization of Cyclin B1 during interphase reflects the equilibrium between ongoing nuclear import and rapid CRM1-mediated export. In support of this hypothesis, we found that treatment of cells with leptomycin B, which disrupted Cyclin B1-CRM1 interactions, led to a marked nuclear accumulation of Cyclin B1. In mitosis, Cyclin B1 undergoes phosphorylation at several sites, a subset of which have been proposed to play a role in Cyclin B1 accumulation in the nucleus. Both CRM1 binding and the ability to direct nuclear export were affected by mutation of these phosphorylation sites; thus, we propose that Cyclin B1 phosphorylation at the G2/M transition prevents its interaction with CRM1, thereby reducing nuclear export and facilitating nuclear accumulation.

Indexed as

Intracellular Signaling Peptides and ProteinsKaryopherinsReceptors, Cytoplasmic and NuclearAnimalsBinding SitesBiological TransportCarrier ProteinsCyclin BCyclin B1Exportin 1 ProteinFatty Acids, UnsaturatedGuanosine DiphosphateHeLa CellsHumansMiceNuclear ProteinsCarrier ProteinsCCNB1 protein, humanCcnb1 protein, mouseCcnb1 protein, ratCyclin BCyclin B1Exportin 1 ProteinFatty Acids, UnsaturatedGuanosine DiphosphateIntracellular Signaling Peptides and ProteinsKaryopherinsleptomycin BNuclear Proteinsprotein kinase modulatorran GTP-Binding ProteinReceptors, Cytoplasmic and NuclearRecombinant Fusion Proteins

Identifiers

PMID9679058
PMCPMC317017
OpenAlexW2119827462

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.