Evidence map›Paper›PMID 10931866›Full record

ArticleThe Journal of cell biology2000

Functional analysis of a human homologue of the Drosophila actin binding protein anillin suggests a role in cytokinesis.

K Oegema, M S Savoian, T J Mitchison, C M Field

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 158 papers.

0numbers the graph read from it
0cells of the map it votes in
158citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

158 citing papers in PubMed, 318 citations in OpenAlex.

  1. Article
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  20. Two Septin Complexes Mediate Actin Dynamics During Cell Wound Repair.bioRxiv : the preprint server for biology · 2023
    Article

98 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

4 authors at 3 institutions in 2 countries.

K OegemaCell Biology Program, European Molecular Biology Laboratory, Heidelberg, Germany D-69117, USA. karen.oegema@embl-heidelerg.de
M S Savoian
T J Mitchison
C M Field
Harvard University · USEuropean Molecular Biology Laboratory · DEWadsworth Center · US

Funding

GENETIC AND BIOCHEMICAL ANALYSIS OF CYTOKINESISR01GM023928 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1985 to 2010
$3.6M
FORMATION, INTERACTION, &FUNCTION OF SPINDLE COMPONENTSR01GM040198 · NIGMS · WADSWORTH CENTER · PI RIEDER, CONLY L. · 1988 to 2000
$206k
NIGMS NIH HHS GM 23928NIGMS NIH HHS GMS RO1 40198NIGMS NIH HHS R01 GM023928
6 · The paper itself

Abstract

We have characterized a human homologue of anillin, a Drosophila actin binding protein. Like Drosophila anillin, the human protein localizes to the nucleus during interphase, the cortex following nuclear envelope breakdown, and the cleavage furrow during cytokinesis. Anillin also localizes to ectopic cleavage furrows generated between two spindles in fused PtK(1) cells. Microinjection of antianillin antibodies slows cleavage, leading to furrow regression and the generation of multinucleate cells. GFP fusions that contain the COOH-terminal 197 amino acids of anillin, which includes a pleckstrin homology (PH) domain, form ectopic cortical foci during interphase. The septin Hcdc10 localizes to these ectopic foci, whereas myosin II and actin do not, suggesting that anillin interacts with the septins at the cortex. Robust cleavage furrow localization requires both this COOH-terminal domain and additional NH(2)-terminal sequences corresponding to an actin binding domain defined by in vitro cosedimentation assays. Endogenous anillin and Hcdc10 colocalize to punctate foci associated with actin cables throughout mitosis and the accumulation of both proteins at the cell equator requires filamentous actin. These results indicate that anillin is a conserved cleavage furrow component important for cytokinesis. Interactions with at least two other furrow proteins, actin and the septins, likely contribute to anillin function.

Indexed as

Cell DivisionAmino Acid SequenceAnimalsBinding SitesBlood ProteinsCell CompartmentationCell Cycle ProteinsConserved SequenceContractile ProteinsDrosophilaEvolution, MolecularHumansMicrofilament ProteinsMolecular Sequence DataPhosphoproteinsProtein Structure, TertiaryanillinBlood ProteinsCell Cycle ProteinsContractile ProteinsMicrofilament ProteinsPhosphoproteinsplatelet protein P47Recombinant Fusion ProteinsSEPTIN7 protein, humanSeptins

Identifiers

PMID10931866
PMCPMC2175195
OpenAlexW2078816010

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.