Evidence map›Paper›PMID 36287824›Full record

ArticleMolecular biology of the cell2022

Imp2p forms actin-dependent clusters and imparts stiffness to the contractile ring.

Kimberly Bellingham-Johnstun, Blake Commer, Brié Levesque, Zoe L Tyree, Caroline Laplante

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 41% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Calcineurin controls the cytokinesis machinery during thermal stress inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
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.

Kimberly Bellingham-JohnstunDepartment of Molecular Biomedical Sciences, North Carolina State University, Raleigh, NC 27607.
Blake CommerDepartment of Molecular Biomedical Sciences, North Carolina State University, Raleigh, NC 27607.
Brié LevesqueDepartment of Molecular Biomedical Sciences, North Carolina State University, Raleigh, NC 27607.
Zoe L TyreeDepartment of Molecular Biomedical Sciences, North Carolina State University, Raleigh, NC 27607.
Caroline LaplanteDepartment of Molecular Biomedical Sciences, North Carolina State University, Raleigh, NC 27607.
North Carolina State University · US

Funding

Tri-Institutional Molecular Mycology and Pathogenesis Training ProgramT32AI052080 · NIAID · DUKE UNIVERSITY · PI ANDREW ALSPAUGH, JOSEPH HEITMAN · 2003 to 2026
$8.7M
Uncovering how the dynamic architecture of a layered contractile ring induces furrow ingressionR01GM134254 · NIGMS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI LAPLANTE, CAROLINE · 2019 to 2023
$1.5M
Mechanisms of force production in cytokinesisR35GM156520 · NIGMS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI Caroline Laplante · 2025 to 2026
$866k
NIAID NIH HHS T32 AI052080NIGMS NIH HHS R01 GM134254NIGMS NIH HHS R35 GM156520
6 · The paper itself

Abstract

The contractile ring must anchor to the plasma membrane and cell wall to transmit its tension. F-BAR domain containing proteins including Imp2p and Cdc15p in fission yeast are likely candidate anchoring proteins based on their mutant phenotypes. Cdc15p is a node component, links the actin bundle to the plasma membrane, recruits Bgs1p to the division plane, prevents contractile ring sliding, and contributes to the stiffness of the contractile ring. Less is known about Imp2p. We found that similarly to Cdc15p, Imp2p contributes to the stiffness of the contractile ring and assembles into protein clusters. Imp2p clusters contain approximately eight Imp2p dimers and depend on the actin network for their stability at the division plane. Importantly, Imp2p and Cdc15p reciprocally affect the amount of each other in the contractile ring, indicating that the two proteins influence each other during cytokinesis, which may partially explain their similar phenotypes.

Indexed as

SchizosaccharomycesSchizosaccharomyces pombe ProteinsActin CytoskeletonActinsCytokinesisCytoskeletal ProteinsActinsCytoskeletal ProteinsIMP2 protein, S pombeSchizosaccharomyces pombe Proteins

Identifiers

PMID36287824
PMCPMC9727792
OpenAlexW4307344497

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.