Evidence map›Paper›PMID 30853434›Full record

ArticleCurrent biology : CB2019

NDR Kinase Sid2 Drives Anillin-like Mid1 from the Membrane to Promote Cytokinesis and Medial Division Site Placement.

Alaina H Willet, Ashley K DeWitt, Janel R Beckley, Dawn M Clifford, Kathleen L Gould

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

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  11. The Role of the Cell Integrity Pathway in Septum Assembly in Yeast.Journal of fungi (Basel, Switzerland) · 2021
    Review
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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 2 institutions in 1 country.

Alaina H WilletDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
Ashley K DeWittGrand Valley State University, Department of Cell and Molecular Biology, Allendale, MI 49401, USA.
Janel R BeckleyDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
Dawn M CliffordGrand Valley State University, Department of Cell and Molecular Biology, Allendale, MI 49401, USA.
Kathleen L GouldDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA. Electronic address: kathy.gould@vanderbilt.edu.
Vanderbilt University · USGrand Valley State University · US

Funding

Checkpoint control of cytokinesisR01GM112989 · NIGMS · VANDERBILT UNIVERSITY · PI GOULD, KATHLEEN L · 2014 to 2017
$1.5M
Mechanisms Regulating Contractile Ring in Fission YeastF32GM076897 · NIGMS · VANDERBILT UNIVERSITY · PI CLIFFORD-HART, DAWN M · 2006 to 2007
$95k
NIGMS NIH HHS F32 GM076897NIGMS NIH HHS R01 GM112989
6 · The paper itself

Abstract

In animals and fungi, cytokinesis is facilitated by the constriction of an actomyosin contractile ring (CR) [1]. In Schizosaccharomyces pombe, the CR forms mid-cell during mitosis from clusters of proteins at the medial cell cortex called nodes [2]. The anillin-like protein Mid1 localizes to nodes and is required for CR assembly at mid-cell [3]. When CR constriction begins, Mid1 leaves the division site. How Mid1 disassociates and whether this step is important for cytokinetic progression has been unknown. The septation initiation network (SIN), analogous to the Hippo pathway of multicellular organisms, is a signaling cascade that triggers node dispersal, CR assembly and constriction, and septum formation [4, 5]. We report that the terminal SIN kinase, Sid2 [6], phosphorylates Mid1 to drive its removal from the cortex at CR constriction onset. A Mid1 mutant that cannot be phosphorylated by Sid2 remains cortical during cytokinesis, over-accumulates in interphase nodes following cell division in a manner dependent on the SAD kinase Cdr2, advances the G2/M transition, precociously recruits other CR components to nodes, pulls Cdr2 aberrantly into the CR, and reduces rates of CR maturation and constriction. When combined with cdr2 mutants that affect node assembly or disassembly, gross defects in division site positioning result. Our findings identify Mid1 as a key Sid2 substrate for SIN-mediated remodeling of the division site for efficient cytokinesis and provide evidence that nodes serve to integrate signals coordinating cell cycle progression and cytokinesis.

Indexed as

Actin CytoskeletonCell Cycle CheckpointsCytokinesisMitosisPhosphorylationProtein KinasesSchizosaccharomycesSchizosaccharomyces pombe ProteinsSignal TransductionMid1 protein, S pombeProtein KinasesSchizosaccharomyces pombe ProteinsSid2 protein, S pombeanillincontractile ringcytokinesisfission yeastnodesSIN signaling

Identifiers

PMID30853434
PMCPMC6424596
OpenAlexW2920797766

What OpenQuestion holds

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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.