ArticleThe Biochemical journal2003
Phosphorylation of myosin II regulatory light chain is necessary for migration of HeLa cells but not for localization of myosin II at the leading edge.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- RhoA through its various effectors mediate mitochondrial fragmentation in polycystic kidney disease.iScience · 2026Article
- Phosphatidylinositol transfer protein/planar cell polarity axis regulates neocortical morphogenesis by supporting interkinetic nuclear migration.Cell reports · 2022Article
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- aPKCζ affects directed cell migration through the regulation of myosin light chain phosphorylation.Cell adhesion & migration · 2017Article
- Release of nonmuscle myosin II from the cytosolic domain of tumor necrosis factor receptor 2 is required for target gene expression.Science signaling · 2013Article
- Relaxin regulates myofibroblast contractility and protects against lung fibrosis.The American journal of pathology · 2011Article
- Slit and Netrin-1 guide cranial motor axon pathfinding via Rho-kinase, myosin light chain kinase and myosin II.Neural development · 2010Article
- A lipid-signaled myosin phosphatase surge disperses cortical contractile force early in cell spreading.Molecular biology of the cell · 2009Article
- The androgen and progesterone receptors regulate distinct gene networks and cellular functions in decidualizing endometrium.Endocrinology · 2008Article
- Article
- Regulation of myosin II dynamics by phosphorylation and dephosphorylation of its light chain in epithelial cells.Molecular biology of the cell · 2007Article
- Traction forces of fibroblasts are regulated by the Rho-dependent kinase but not by the myosin light chain kinase.Archives of biochemistry and biophysics · 2006Article
- Actin and non-muscle myosin II facilitate apical exocytosis of tear proteins in rabbit lacrimal acinar epithelial cells.Journal of cell science · 2005Article
- Redundant mechanisms for anaphase chromosome movements: crane-fly spermatocyte spindles normally use actin filaments but also can function without them.Protoplasma · 2005Article
- DRhoGEF2 regulates actin organization and contractility in the Drosophila blastoderm embryo.The Journal of cell biology · 2005Article
- Asymmetric distribution of myosin IIB in migrating endothelial cells is regulated by a rho-dependent kinase and contributes to tail retraction.Molecular biology of the cell · 2003Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To investigate the role of phosphorylated myosin II regulatory light chain (MRLC) in living cell migration, these mutant MRLCs were engineered and introduced into HeLa cells. The mutant MRLCs include an unphosphorylatable form, in which both Thr-18 and Ser-19 were substituted with Ala (AA-MRLC), and pseudophosphorylated forms, in which Thr-18 and Ser-19 were replaced with Ala and Asp, respectively (AD-MRLC), and both Thr-18 and Ser-19 were replaced with Asp (DD-MRLC). Mutant MRLC-expressing cell monolayers were mechanically stimulated by scratching, and the cells were forced to migrate in a given direction. In this wound-healing assay, the AA-MRLC-expressing cells migrated much more slowly than the wild-type MRLC-expressing cells. In the case of DD-MRLC- and AD-MRLC-expressing cells, no significant differences compared with wild-type MRLC-expressing cells were observed in their migration speed. Indirect immunofluorescence staining showed that the accumulation of endogenous diphosphorylated MRLC at the leading edge was not observed in AA-MRLC-expressing cells, although AA-MRLC was incorporated into myosin heavy chain and localized at the leading edge. In conclusion, we propose that the phosphorylation of MRLC is required to generate the driving force in the migration of the cells but not necessary for localization of myosin II at the leading edge.
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