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

Author: C Chen Affiliation: From the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.T Tao Affiliation: From the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.C Wen Affiliation: School 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.WQ He Affiliation: From the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.YN Qiao Affiliation: From the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.All authors
Edition/Format: Article Article : English
Publication:The Journal of biological chemistry, 2014 Oct 10; 289(41): 28478-88
Summary:
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  Read more...
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Document Type: Article
All Authors / Contributors: C Chen Affiliation: From the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.; T Tao Affiliation: From the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.; C Wen Affiliation: School 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.; WQ He Affiliation: From the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.; YN Qiao Affiliation: From the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.; YQ Gao Affiliation: From the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.; X Chen Affiliation: From the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.; P Wang Affiliation: From the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.; CP Chen Affiliation: From the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.; W Zhao Affiliation: From the Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing 210061, P.R. China.; HQ Chen Affiliation: School of Life Science, Nanjing Normal University, Nanjing 210009, P.R. China.; AP Ye Affiliation: School 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.; YJ Peng Affiliation: From 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.; MS Zhu Affiliation: From 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.
ISSN:0021-9258
Language Note: English
Unique Identifier: 5665955378
Awards:

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.

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