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- W2498148718 endingPage "97" @default.
- W2498148718 startingPage "79" @default.
- W2498148718 abstract "This chapter discusses normal and pathophysiological significance of myotonic dystrophy protein kinase (DMPK). DMPK is a member of the group of AGC kinases, which is mainly expressed in heart, skeletal and smooth muscle, and brain. The structure, enzymatic activity, and subcellular localization of DMPK protein isoforms are strongly dictated by alternative splicing, which results in cell-type dependent expression of distinct isoforms, which partition in a species-dependent manner across cytosol, endoplasmic reticulum (ER), and the mitochondria. All DMPKs share a Leu-rich N-terminal leader segment, a typical kinase domain with Lys/Arg directed serine/threonine substrate specificity, and a coiled-coil domain involved in protein multimerization. Isoforms differ in absence/presence of an internal VSGGG motif and tails with motifs that serve as a specific C-terminal anchors for ER and MOM. Cell biological and bioinformatic studies, including functional and structural homology comparison to related kinases, suggest that DMPKs may be regulators of mitochondrial dynamics, actin-cytoskeleton dynamics, and ion homeostasis. Clearly, these are processes with specific relevance for muscle and brain, the main targets of disease in DM1 patients. Moreover, transgenic mouse and cell-model studies point out that strict control of DMPK expression is important for cellular viability and function." @default.
- W2498148718 created "2016-08-23" @default.
- W2498148718 creator A5004158501 @default.
- W2498148718 creator A5007959214 @default.
- W2498148718 creator A5060858832 @default.
- W2498148718 date "2006-01-01" @default.
- W2498148718 modified "2023-09-26" @default.
- W2498148718 title "Normal and Pathophysiological Significance of Myotonic Dystrophy Protein Kinase" @default.
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