Evidence map›Paper›PMID 11815633›Full record

ArticleThe Journal of cell biology2002

A fluorescent resonant energy transfer-based biosensor reveals transient and regional myosin light chain kinase activation in lamella and cleavage furrows.

Teng-Leong Chew, Wendy A Wolf, Patricia J Gallagher, Fumio Matsumura, Rex L Chisholm

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

43 citing papers in PubMed, 117 citations in OpenAlex.

  1. A Constellation of Fluorescent Biosensors to Illuminate the Galaxy of Protein Kinases.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Review
  3. Collagen fiber structure guides 3D motility of cytotoxic T lymphocytes.Matrix biology : journal of the International Society for Matrix Biology · 2020
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  18. Nonmuscle myosin-2: mix and match.Cellular and molecular life sciences : CMLS · 2013
    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 4 institutions in 1 country.

Teng-Leong ChewDepartment of Cell and Molecular Biology, R.H. Lurie Comprehensive Cancer Center and Center for Genetic Medicine, Northwestern University Medical School, Chicago, IL 60611, USA.
Wendy A Wolf
Patricia J Gallagher
Fumio Matsumura
Rex L Chisholm
Northwestern University · USIndiana University School of MedicineRobert H. Lurie Comprehensive Cancer Center of Northwestern UniversityRutgers, The State University of New Jersey · US

Funding

MOLECULAR GENETIC ANALYSIS OF MOTILITY: MYOSIN LCSR01GM039264 · NIGMS · NORTHWESTERN UNIVERSITY · PI CHISHOLM, REX L · 1988 to 2002
$1.0M
NIGMS NIH HHS GM39264NIGMS NIH HHS R01 GM039264
6 · The paper itself

Abstract

Approaches with high spatial and temporal resolution are required to understand the regulation of nonmuscle myosin II in vivo. Using fluorescence resonance energy transfer we have produced a novel biosensor allowing simultaneous determination of myosin light chain kinase (MLCK) localization and its [Ca2+]4/calmodulin-binding state in living cells. We observe transient recruitment of diffuse MLCK to stress fibers and its in situ activation before contraction. MLCK is highly active in the lamella of migrating cells, but not at the retracting tail. This unexpected result highlights a potential role for MLCK-mediated myosin contractility in the lamella as a driving force for migration. During cytokinesis, MLCK was enriched at the spindle equator during late metaphase, and was maximally activated just before cleavage furrow constriction. As furrow contraction was completed, active MLCK was redistributed to the poles of the daughter cells. These results show MLCK is a myosin regulator in the lamella and contractile ring, and pinpoints sites where myosin function may be mediated by other kinases.

Indexed as

AnimalsBiosensing TechniquesCalciumCalcium SignalingCalmodulinCell DivisionCell MovementCell PolarityCytoskeletonDipodomysIntracellular MembranesMicroscopy, FluorescenceMyosin-Light-Chain KinaseMyosinsPseudopodiaCalciumCalmodulinMyosin-Light-Chain KinaseMyosins

Identifiers

PMID11815633
PMCPMC2173328
OpenAlexW2134848551

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.