Alternative Splicing Controls Myotonic Dystrophy Protein Kinase Structure, Enzymatic Activity, and Subcellular Localization

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Published inMolecular and Cellular Biology Vol. 23; no. 16; pp. 5489 - 5501
Main Authors Wansink, Derick G., van Herpen, René E. M. A., Coerwinkel-Driessen, Marga M., Groenen, Patricia J. T. A., Hemmings, Brian A., Wieringa, Bé
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.08.2003
Taylor & Francis
Subjects
Online AccessGet full text
ISSN0270-7306
1098-5549
1067-8824
1098-5549
DOI10.1128/MCB.23.16.5489-5501.2003

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Abstract 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       
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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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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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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StartPage 5489
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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https://pubmed.ncbi.nlm.nih.gov/PMC166319
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