Evidence map›Paper›PMID 25959226›Full record

ArticleDevelopmental cell2015

Mechanistic insights into the anchorage of the contractile ring by anillin and Mid1.

Lingfei Sun, Ruifang Guan, I-Ju Lee, Yajun Liu, Mengran Chen, Jiawei Wang, Jian-Qiu Wu, Zhucheng Chen

Abstract read
In one paragraph

Article in Developmental cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

78 citing papers in PubMed, 140 citations in OpenAlex.

  1. Local PI(4,5)PNature communications · 2026
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  16. Two Septin Complexes Mediate Actin Dynamics During Cell Wound Repair.bioRxiv : the preprint server for biology · 2023
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18 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

8 authors at 2 institutions in 2 countries.

Lingfei SunMOE Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China; School of Life Science, Tsinghua University, Beijing 100084, China.
Ruifang GuanMOE Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China; School of Life Science, Tsinghua University, Beijing 100084, China.
I-Ju LeeDepartment of Molecular Genetics, The Ohio State University, Columbus, OH 43210, USA.
Yajun LiuDepartment of Molecular Genetics, The Ohio State University, Columbus, OH 43210, USA.
Mengran ChenMOE Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China; School of Life Science, Tsinghua University, Beijing 100084, China.
Jiawei WangSchool of Life Science, Tsinghua University, Beijing 100084, China; State Key Laboratory of Bio-membrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China.
Jian-Qiu WuDepartment of Molecular Genetics, The Ohio State University, Columbus, OH 43210, USA.
Zhucheng ChenMOE Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China; School of Life Science, Tsinghua University, Beijing 100084, China. Electronic address: zhucheng_chen@tsinghua.edu.cn.
Tsinghua University · CNThe Ohio State University · US

Funding

Molecular Mechanism of the Contractile-Ring Assembly in Fission Yeast CytokinesisR01GM086546 · NIGMS · OHIO STATE UNIVERSITY · PI WU, JIAN-QIU · 2009 to 2013
$1.4M
NIGMS NIH HHS GM086546NIGMS NIH HHS R01 GM086546
6 · The paper itself

Abstract

Anillins and Mid1 are scaffold proteins that play key roles in anchorage of the contractile ring at the cell equator during cytokinesis in animals and fungi, respectively. Here, we report crystal structures and functional analysis of human anillin and S. pombe Mid1. The combined data show anillin contains a cryptic C2 domain and a Rho-binding domain. Together with the tethering PH domain, three membrane-associating elements synergistically bind to RhoA and phospholipids to anchor anillin at the cleavage furrow. Surprisingly, Mid1 also binds to the membrane through a cryptic C2 domain. Dimerization of Mid1 leads to high affinity and preference for PI(4,5)P2, which stably anchors Mid1 at the division plane, bypassing the requirement for Rho GTPase. These findings uncover the unexpected general machinery and the divergent regulatory logics for the anchorage of the contractile ring through the anillin/Mid1 family proteins from yeast to humans.

Indexed as

Actin CytoskeletonAmino Acid SequenceCell MembraneCrystallography, X-RayCytokinesisHumansMicrofilament ProteinsMolecular Sequence DataPhospholipidsProtein Structure, TertiaryrhoA GTP-Binding ProteinSchizosaccharomyces pombe ProteinsANLN protein, humanMicrofilament ProteinsMid1 protein, S pombePhospholipidsrhoA GTP-Binding ProteinSchizosaccharomyces pombe Proteins

Identifiers

PMID25959226
PMCPMC4449299
OpenAlexW1941858603

What OpenQuestion holds

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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.