Abnormal actomyosin assembly in proliferating and differentiating myoblasts upon expression of a cytosolic DMPK isoform

Autor: Miranda B. Bennink, Susan A. M. Mulders, Mietske Wijers, Jack A.M. Fransen, Remco van Horssen, Fons A. J. van de Loo, Bé Wieringa, Roelie T. de Boer-van Huizen, Lieke Gerrits, H.J.E. Croes, Helma Pluk, Derick G. Wansink
Rok vydání: 2011
Předmět:
Gene isoform
Stress fiber
Myotonic dystrophy protein kinase
Biology
Protein Serine-Threonine Kinases
Muscle Development
Myotonin-Protein Kinase
Myoblasts
Mice
Cytosol
Immune Regulation [NCMLS 2]
Cell Movement
Stress Fibers
ROCK
Myocyte
Animals
Rho kinase
Phosphorylation
Cytoskeleton
Protein Structure
Quaternary
Cell Shape
Molecular Biology
Actin
Cell Proliferation
Myosin Type II
Myogenesis
Alternative splicing
Actomyosin cytoskeleton
Cell Polarity
Cell Differentiation
Actomyosin
Cell Biology
Infection and autoimmunity Auto-immunity
transplantation and immunotherapy [NCMLS 1]
Actins
Isoenzymes
Protein Transport
Biochemistry
Evaluation of complex medical interventions Auto-immunity
transplantation and immunotherapy [NCEBP 2]
Energy and redox metabolism Mitochondrial medicine [NCMLS 4]
Infection and autoimmunity [NCMLS 1]
Subcellular Fractions
Zdroj: Biochimica et Biophysica Acta. Molecular Cell Research, 1813, 5, pp. 867-77
Biochimica et Biophysica Acta. Molecular Cell Research, 1813, 867-77
ResearcherID
ISSN: 0167-4889
DOI: 10.1016/j.bbamcr.2011.01.024
Popis: Contains fulltext : 97603.pdf (Publisher’s version ) (Closed access) DMPK, the product of the mutated gene in myotonic dystrophy type 1, belongs to the subfamily of Rho-associated serine-threonine protein kinases, whose members play a role in actin-based cell morphodynamics. Not much is known about the physiological role of differentially localized individual DMPK splice isoforms. We report here that prominent stellar-shaped stress fibers are formed during early and late steps of differentiation in DMPK-deficient myoblast-myotubes upon complementation with the short cytosolic DMPK E isoform. Expression of DMPK E led to an increased phosphorylation status of MLC2. We found no such effects with vectors that encode a mutant DMPK E which was rendered enzymatically inactive or any of the long C-terminally anchored DMPK isoforms. Presence of stellar structures appears associated with changes in cell shape and motility and a delay in myogenesis. Our data strongly suggest that cytosolic DMPK participates in remodeling of the actomyosin cytoskeleton in developing skeletal muscle cells. This article is part of a Special Issue entitled: 11th European Symposium on Calcium.
Databáze: OpenAIRE
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