Evidence map›Paper›PMID 25122766›Full record

ArticleThe Journal of biological chemistry2014

Myosin light chain kinase (MLCK) regulates cell migration in a myosin regulatory light chain phosphorylation-independent mechanism.

Chen Chen, Tao Tao, Cheng Wen, Wei-Qi He, Yan-Ning Qiao, Yun-Qian Gao, Xin Chen, Pei Wang, Cai-Ping Chen, Wei Zhao and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Regulation of Cancer Metastasis by PAK2.International journal of molecular sciences · 2024
    Review
  3. Article
  4. Article
  5. Myosin Light-Chain Kinase Inhibition Potentiates the Antitumor Effects of Avapritinib in PDGFRA D842V-Mutant Gastrointestinal Stromal Tumor.Clinical cancer research : an official journal of the American Association for Cancer Research · 2023
    Article
  6. Article
  7. Article
  8. FAK in Cancer: From Mechanisms to Therapeutic Strategies.International journal of molecular sciences · 2022
    Review
  9. Article
  10. Article
  11. Review
  12. Ion Channels in Glioma Malignancy.Reviews of physiology, biochemistry and pharmacology · 2021
    Review
  13. Article
  14. Myosin light chain kinase is a potential target for hypopharyngeal cancer treatment.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2020
    Article
  15. CaAdvances in cancer research · 2020
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Role of KCa3.1 Channels in Modulating CaInternational journal of molecular sciences · 2018
    Review
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

14 authors at 4 institutions in 1 country.

Chen ChenFrom the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.
Tao TaoFrom the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.
Cheng WenSchool of Electronics Engineering and Computer Science, Key Laboratory for the Physics & Chemistry of Nanodevices of Ministry of Education, Peking University, Beijing 100871, P.R. China, and.
Wei-Qi HeFrom the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.
Yan-Ning QiaoFrom the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.
Yun-Qian GaoFrom the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.
Xin ChenFrom the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.
Pei WangFrom the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.
Cai-Ping ChenFrom the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.
Wei ZhaoFrom the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.
Hua-Qun ChenSchool of Life Science, Nanjing Normal University, Nanjing 210009, P.R. China.
An-Pei YeSchool of Electronics Engineering and Computer Science, Key Laboratory for the Physics & Chemistry of Nanodevices of Ministry of Education, Peking University, Beijing 100871, P.R. China, and.
Ya-Jing PengFrom the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China, pengyj@nicemice.cn.
Min-Sheng ZhuFrom the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China, School of Life Science, Nanjing Normal University, Nanjing 210009, P.R. China zhums@nju.edu.cn.
Nanjing University · CNPeking University · CNModel Animal Research Center · CNNanjing Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myosin light chain kinase (MLCK) has long been implicated in the myosin phosphorylation and force generation required for cell migration. Here, we surprisingly found that the deletion of MLCK resulted in fast cell migration, enhanced protrusion formation, and no alteration of myosin light chain phosphorylation. The mutant cells showed reduced membrane tether force and fewer membrane F-actin filaments. This phenotype was rescued by either kinase-dead MLCK or five-DFRXXL motif, a MLCK fragment with potent F-actin-binding activity. Pull-down and co-immunoprecipitation assays showed that the absence of MLCK led to attenuated formation of transmembrane complexes, including myosin II, integrins and fibronectin. We suggest that MLCK is not required for myosin phosphorylation in a migrating cell. A critical role of MLCK in cell migration involves regulating the cell membrane tension and protrusion necessary for migration, thereby stabilizing the membrane skeleton through F-actin-binding activity. This finding sheds light on a novel regulatory mechanism of protrusion during cell migration.

Indexed as

Actin CytoskeletonActinsAdenoviridaeAmino Acid MotifsAnimalsCell MembraneCell MovementGene Expression RegulationGenetic VectorsJejunumMiceMice, KnockoutMolecular Sequence DataMyocytes, Smooth MuscleMyosin-Light-Chain KinasePhosphorylationActinsMyosin-Light-Chain KinaseActinCell MigrationCell MotilityCortical CytoskeletonCytoskeletonMembrane ProtrusionMembrane TensionMyosinMyosin Light Chain KinasePlasma Membrane

Identifiers

PMID25122766
PMCPMC4192498
OpenAlexW2116098498

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.