Alternative Splicing Controls Myotonic Dystrophy Protein Kinase Structure, Enzymatic Activity, and Subcellular Localization
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Published in | Molecular and Cellular Biology Vol. 23; no. 16; pp. 5489 - 5501 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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01.08.2003
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ISSN | 0270-7306 1098-5549 1067-8824 1098-5549 |
DOI | 10.1128/MCB.23.16.5489-5501.2003 |
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AbstractList | Transcripts of the myotonic dystrophy protein kinase (DMPK) gene, a member of the Rho kinase family, are subject to cell-type specific alternative splicing. An imbalance in the splice isoform profile of DMPK may play a role in the pathogenesis of DM1, a severe multisystemic disorder. Here, we report how structural subdomains determine biochemical properties and subcellular distribution of DMPK isoforms. A newly developed kinase assay revealed that DMPK is a Lys/Arg-directed kinase. Individual DMPK isoforms displayed comparable transphosphorylation activity and sequence preference for peptide substrates. However, DMPK autophosphorylation and phosphorylation of MYPT1 (as putative in vivo target of DMPK), were dependent on presence of an alternatively spliced VSGGG motif and the nature of the C terminus. In-gel effects of the VSGGG motif on the migration behavior of full-length kinase provide evidence for a model in which this motif mediates 3-D-conformational changes in DMPK isoforms. Finally, different C termini endow DMPK with the ability to bind to either endoplasmic reticulum or mitochondria or to adopt a cytosolic location. Our results suggest that DMPK isoforms have cell-type and location dependent substrate specificities with a role in organellar and cytoarchitectural dynamics. Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology. For an alternate route to MCB .asm.org, visit: MCB Transcripts of the myotonic dystrophy protein kinase (DMPK) gene, a member of the Rho kinase family, are subject to cell-type specific alternative splicing. An imbalance in the splice isoform profile of DMPK may play a role in the pathogenesis of DM1, a severe multisystemic disorder. Here, we report how structural subdomains determine biochemical properties and subcellular distribution of DMPK isoforms. A newly developed kinase assay revealed that DMPK is a Lys/Arg-directed kinase. Individual DMPK isoforms displayed comparable transphosphorylation activity and sequence preference for peptide substrates. However, DMPK autophosphorylation and phosphorylation of MYPT1 (as putative in vivo target of DMPK), were dependent on presence of an alternatively spliced VSGGG motif and the nature of the C terminus. In-gel effects of the VSGGG motif on the migration behavior of full-length kinase provide evidence for a model in which this motif mediates 3-D-conformational changes in DMPK isoforms. Finally, different C termini endow DMPK with the ability to bind to either endoplasmic reticulum or mitochondria or to adopt a cytosolic location. Our results suggest that DMPK isoforms have cell-type and location dependent substrate specificities with a role in organellar and cytoarchitectural dynamics.Transcripts of the myotonic dystrophy protein kinase (DMPK) gene, a member of the Rho kinase family, are subject to cell-type specific alternative splicing. An imbalance in the splice isoform profile of DMPK may play a role in the pathogenesis of DM1, a severe multisystemic disorder. Here, we report how structural subdomains determine biochemical properties and subcellular distribution of DMPK isoforms. A newly developed kinase assay revealed that DMPK is a Lys/Arg-directed kinase. Individual DMPK isoforms displayed comparable transphosphorylation activity and sequence preference for peptide substrates. However, DMPK autophosphorylation and phosphorylation of MYPT1 (as putative in vivo target of DMPK), were dependent on presence of an alternatively spliced VSGGG motif and the nature of the C terminus. In-gel effects of the VSGGG motif on the migration behavior of full-length kinase provide evidence for a model in which this motif mediates 3-D-conformational changes in DMPK isoforms. Finally, different C termini endow DMPK with the ability to bind to either endoplasmic reticulum or mitochondria or to adopt a cytosolic location. Our results suggest that DMPK isoforms have cell-type and location dependent substrate specificities with a role in organellar and cytoarchitectural dynamics. |
Author | Marga M. Coerwinkel-Driessen Brian A. Hemmings Derick G. Wansink René E. M. A. van Herpen Bé Wieringa Patricia J. T. A. Groenen |
AuthorAffiliation | Department of Cell Biology, Nijmegen Center for Molecular Life Sciences, University Medical Center, 6500 HB Nijmegen, The Netherlands, 1 Friedrich Miescher Institute, CH-4058 Basel, Switzerland 2 |
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Author_xml | – sequence: 1 givenname: Derick G. surname: Wansink fullname: Wansink, Derick G. email: r.wansink@ncmls.kun.nl organization: Department of Cell Biology, Nijmegen Center for Molecular Life Sciences, University Medical Center – sequence: 2 givenname: René E. M. A. surname: van Herpen fullname: van Herpen, René E. M. A. organization: Department of Cell Biology, Nijmegen Center for Molecular Life Sciences, University Medical Center – sequence: 3 givenname: Marga M. surname: Coerwinkel-Driessen fullname: Coerwinkel-Driessen, Marga M. organization: Department of Cell Biology, Nijmegen Center for Molecular Life Sciences, University Medical Center – sequence: 4 givenname: Patricia J. T. A. surname: Groenen fullname: Groenen, Patricia J. T. A. organization: Department of Cell Biology, Nijmegen Center for Molecular Life Sciences, University Medical Center – sequence: 5 givenname: Brian A. surname: Hemmings fullname: Hemmings, Brian A. organization: Friedrich Miescher Institute – sequence: 6 givenname: Bé surname: Wieringa fullname: Wieringa, Bé organization: Department of Cell Biology, Nijmegen Center for Molecular Life Sciences, University Medical Center |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/12897125$$D View this record in MEDLINE/PubMed |
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Notes | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 Corresponding author. Mailing address: Department of Cell Biology (163), Nijmegen Center for Molecular Life Sciences, University Medical Center, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands. Phone: 31.24.3613664. Fax: 31.24.3615317. E-mail: r.wansink@ncmls.kun.nl. Present address: Department of Pathology, University Medical Center, 6500 HB Nijmegen, The Netherlands. |
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Mendeley... Transcripts of the myotonic dystrophy protein kinase (DMPK) gene, a member of the Rho kinase family, are subject to cell-type specific alternative splicing. An... |
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SubjectTerms | Alternative Splicing Amino Acid Motifs Amino Acid Sequence Animals Blotting, Western Cell Growth and Development Cell Movement COS Cells Cytosol - metabolism DNA, Complementary - metabolism Electrophoresis, Polyacrylamide Gel Endoplasmic Reticulum - metabolism Mice Microscopy, Fluorescence Mitochondria - metabolism Models, Biological Models, Genetic Molecular Sequence Data Mutation Myosin-Light-Chain Phosphatase Myotonin-Protein Kinase Phosphoprotein Phosphatases - chemistry Phosphoprotein Phosphatases - genetics Phosphorylation Plasmids - metabolism Precipitin Tests Protein Conformation Protein Isoforms Protein Structure, Tertiary Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - genetics Sequence Homology, Amino Acid |
Title | Alternative Splicing Controls Myotonic Dystrophy Protein Kinase Structure, Enzymatic Activity, and Subcellular Localization |
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