A 3.7kb fragment from the myotonic dystrophy protein kinase promoter directs neural-specific expression in vivo

1996 ◽  
Vol 24 (2) ◽  
pp. 283S-283S ◽  
Author(s):  
STEPHANIE K. KING ◽  
DOMINIC J. WELLS ◽  
KIM E. WELLS ◽  
NESSA CAREY ◽  
KEITH J. JOHNSON
Keyword(s):  
Protein Kinase ◽  
Myotonic Dystrophy ◽  
Specific Expression ◽  
Myotonic Dystrophy Protein Kinase

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

2003 ◽  
Vol 23 (16) ◽  
pp. 5489-5501 ◽  
Author(s):  
Derick G. Wansink ◽  
René E. M. A. van Herpen ◽  
Marga M. Coerwinkel-Driessen ◽  
Patricia J. T. A. Groenen ◽  
Brian A. Hemmings ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Protein Kinase ◽  
Myotonic Dystrophy ◽  
Conformational Changes ◽  
Biochemical Properties ◽  
Kinase Assay ◽  
Migration Behavior ◽  
Cell Type ◽  
Myotonic Dystrophy Protein Kinase

ABSTRACT 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.

Developmental regulation of myotonic dystrophy protein kinase in human muscle cells in vitro

Neuroscience ◽  
1998 ◽  
Vol 85 (1) ◽  
pp. 311-322 ◽  
Author(s):  
N Kameda ◽  
H Ueda ◽  
S Ohno ◽  
M Shimokawa ◽  
F Usuki ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Myotonic Dystrophy ◽  
Developmental Regulation ◽  
Muscle Cells ◽  
Human Muscle ◽  
Myotonic Dystrophy Protein Kinase ◽  
Human Muscle Cells

scholarly journals A Tail-Anchored Myotonic Dystrophy Protein Kinase Isoform Induces Perinuclear Clustering of Mitochondria, Autophagy, and Apoptosis

PLoS ONE ◽  
2009 ◽  
Vol 4 (11) ◽  
pp. e8024 ◽  
Author(s):  
Ralph J. A. Oude Ophuis ◽  
Mietske Wijers ◽  
Miranda B. Bennink ◽  
Fons A. J. van de Loo ◽  
Jack A. M. Fransen ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Myotonic Dystrophy ◽  
Myotonic Dystrophy Protein Kinase

Myotonic Dystrophy Protein Kinase Domains Mediate Localization, Oligomerization, Novel Catalytic Activity, and Autoinhibition†

Biochemistry ◽  
2000 ◽  
Vol 39 (29) ◽  
pp. 8480-8490 ◽  
Author(s):  
Erik W. Bush ◽  
Steve M. Helmke ◽  
Richard A. Birnbaum ◽  
M. Benjamin Perryman
Keyword(s):  
Catalytic Activity ◽  
Protein Kinase ◽  
Myotonic Dystrophy ◽  
Myotonic Dystrophy Protein Kinase
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