Evidence map›Paper›PMID 17050732›Full record

ArticleMolecular biology of the cell2006

Enlazin, a natural fusion of two classes of canonical cytoskeletal proteins, contributes to cytokinesis dynamics.

Edelyn Octtaviani, Janet C Effler, Douglas N Robinson

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

26 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Cytokinesis: Robust cell shape regulation.Seminars in cell & developmental biology · 2016
    Review
  8. Article
  9. Article
  10. Article
  11. Cytokinesis mechanics and mechanosensing.Cytoskeleton (Hoboken, N.J.) · 2012
    Review
  12. Article
  13. Article
  14. Cytokinesis through biochemical-mechanical feedback loops.Seminars in cell & developmental biology · 2010
    Review
  15. Article
  16. The FERM domain: organizing the structure and function of FAK.Nature reviews. Molecular cell biology · 2010
    Review
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Edelyn OcttavianiDepartment of Cell Biology, Johns Hopkins School of Medicine, Baltimore, MD 21205, USA.
Janet C Effler
Douglas N Robinson
Johns Hopkins University · US

Funding

The Biochemical Basis for the Mechanics of CytokinesisR01GM066817 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROBINSON, DOUGLAS N · 2003 to 2025
$7.3M
NIGMS NIH HHS R01 GM-066817NIGMS NIH HHS R01 GM066817
6 · The paper itself

Abstract

Cytokinesis requires a complex network of equatorial and global proteins to regulate cell shape changes. Here, using interaction genetics, we report the first characterization of a novel protein, enlazin. Enlazin is a natural fusion of two canonical classes of actin-associated proteins, the ezrin-radixin-moesin family and fimbrin, and it is localized to actin-rich structures. A fragment of enlazin, enl-tr, was isolated as a genetic suppressor of the cytokinesis defect of cortexillin-I mutants. Expression of enl-tr disrupts expression of endogenous enlazin, indicating that enl-tr functions as a dominant-negative lesion. Enlazin is distributed globally during cytokinesis and is required for cortical tension and cell adhesion. Consistent with a role in cell mechanics, inhibition of enlazin in a cortexillin-I background restores cytokinesis furrowing dynamics and suppresses the growth-in-suspension defect. However, as expected for a role in cell adhesion, inhibiting enlazin in a myosin-II background induces a synthetic cytokinesis phenotype, frequently arresting furrow ingression at the dumbbell shape and/or causing recession of the furrow. Thus, enlazin has roles in cell mechanics and adhesion, and these roles seem to be differentially significant for cytokinesis, depending on the genetic background.

Indexed as

CytokinesisAmino Acid SequenceAnimalsBiomechanical PhenomenaCell AdhesionCell Growth ProcessesCytoskeletal ProteinsDictyosteliumGene SilencingMicrofilament ProteinsMolecular Sequence DataMutationPeptide FragmentsPhenotypeProtozoan ProteinsctxA protein, Dictyostelium discoideumCytoskeletal ProteinsMicrofilament ProteinsPeptide FragmentsProtozoan Proteins

Identifiers

PMID17050732
PMCPMC1679690
OpenAlexW2122401346

What OpenQuestion holds

Textmetadata
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.