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 |
Externí odkaz: |