Nuclear localization of Myomesin-1: possible functions
| Autor: | Sudhiranjan Gupta, Maureen G. Price, Biswajit Das, Kumar B. Reddy, Joan E.B. Fox, Dawn M. Smith, Sucheta Kulkarni |
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| Rok vydání: | 2008 |
| Předmět: |
Sarcomeres
Physiology Down-Regulation Muscle Proteins CHO Cells Transfection Biochemistry Sarcomere Cell Line Rats Sprague-Dawley Mice Cricetulus Cricetinae Myosin Consensus sequence medicine Myocyte Animals Humans Connectin Myocytes Cardiac Muscle Skeletal Oligonucleotide Array Sequence Analysis Myomesin Cell Nucleus biology Gene Expression Profiling Cell Biology Molecular biology Cell biology Rats Up-Regulation Cytoskeletal Proteins medicine.anatomical_structure Animals Newborn Cytoplasm biology.protein Nucleus Nuclear localization sequence |
| Zdroj: | Journal of muscle research and cell motility. 29(1) |
| ISSN: | 0142-4319 |
| Popis: | Myomesin-I (also known as Skelemin) is a approximately 185 kDa protein, which is highly expressed in striated muscle. It contains the prototypic class-I (type-III fibronectin) and class-II (C2-immunoglobulin) motifs. Previous studies have shown the presence of Myomesin-I at the M-line of the sarcomere, where it is thought to interact with thick filament constituents. As reported previously, Myomesin-I was localized to the M-line in the adult cardiac myocytes (adult-myocytes). However, we found that Myomesin-I was also present exclusively in the nucleus of myocytes isolated from new born pups (neonatal-myocytes). In addition, the ectopically expressed Myomesin-I was primarily targeted to the nucleus, similar to the neonatal myocytes. Further investigations revealed that the nuclear-targeting signals were present within the N-terminal 256 residues. A strong consensus sequence for sumoylation is present within the N-terminal 256 residues and is implicated in the shuttling of Myomesin-I between nucleus and cytoplasm. Gene array analysis showed that the presence of Myomesin-I in the nucleus led to the differential expression of more than 42 genes. These studies show a novel and previously unknown localization and function for Myomesin-I. |
| Databáze: | OpenAIRE |
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