Evidence map›Paper›PMID 28081137›Full record

ArticlePLoS genetics2017

Anillin Phosphorylation Controls Timely Membrane Association and Successful Cytokinesis.

Hyunjung Kim, James M Johnson, Robert F Lera, Sarang Brahma, Mark E Burkard

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

25 citing papers in PubMed, 43 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

5 authors at 1 institution in 1 country.

Hyunjung KimUniversity of Wisconsin Carbone Cancer Center and Department of Medicine, Hematology/Oncology, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.
James M JohnsonUniversity of Wisconsin Carbone Cancer Center and Department of Medicine, Hematology/Oncology, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.
Robert F LeraUniversity of Wisconsin Carbone Cancer Center and Department of Medicine, Hematology/Oncology, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.ORCID http://orcid.org/0000-0001-8713-4279
Sarang BrahmaUniversity of Wisconsin Carbone Cancer Center and Department of Medicine, Hematology/Oncology, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.
Mark E BurkardUniversity of Wisconsin Carbone Cancer Center and Department of Medicine, Hematology/Oncology, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.
University of Wisconsin–Madison · US

Funding

UW COMPREHENSIVE CANCER CENTER SUPPORTP30CA014520 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI AMY TRENTHAM-DIETZ · 1985 to 2026
$142.6M
Viral VectorP30CA086862 · NCI · UNIVERSITY OF IOWA · PI Douglas Robert Spitz · 2000 to 2026
$70.0M
Separation of late mitotic functions of polo-like kinase 1 with chemical geneticsR01GM097245 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BURKARD, MARK E · 2011 to 2015
$1.4M
NCI NIH HHS P30 CA014520NCI NIH HHS P30 CA086862NIGMS NIH HHS R01 GM097245
6 · The paper itself

Abstract

During cytokinesis, a contractile ring generates the constricting force to divide a cell into two daughters. This ring is composed of filamentous actin and the motor protein myosin, along with additional structural and regulatory proteins, including anillin. Anillin is a required scaffold protein that links the actomyosin ring to membrane and its organizer, RhoA. However, the molecular basis for timely action of anillin at cytokinesis remains obscure. Here, we find that phosphorylation regulates efficient recruitment of human anillin to the equatorial membrane. Anillin is highly phosphorylated in mitosis, and is a substrate for mitotic kinases. We surveyed function of 46 residues on anillin previously found to be phosphorylated in human cells to identify those required for cytokinesis. Among these sites, we identified S635 as a key site mediating cytokinesis. Preventing S635 phosphorylation adjacent to the AH domain disrupts anillin concentration at the equatorial cortex at anaphase, whereas a phosphomimetic mutant, S635D, partially restores this localization. Time-lapse videomicroscopy reveals impaired recruitment of S635A anillin to equatorial membrane and a transient unstable furrow followed by ultimate failure in cytokinesis. A phosphospecific antibody confirms phosphorylation at S635 in late cytokinesis, although it does not detect phosphorylation in early cytokinesis, possibly due to adjacent Y634 phosphorylation. Together, these findings reveal that anillin recruitment to the equatorial cortex at anaphase onset is enhanced by phosphorylation and promotes successful cytokinesis.

Indexed as

CytokinesisProtein Processing, Post-TranslationalCell MembraneHeLa CellsHumansMicrofilament ProteinsMutationPhosphorylationANLN protein, humanMicrofilament Proteins

Identifiers

PMID28081137
PMCPMC5230765
OpenAlexW2573530718

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.