Alternative splicing of (ppp1r12a/mypt1) in zebrafish produces a novel myosin phosphatase targeting subunit
| Autor: | Kyle E. Young, Irene Lang, Douglas C. Weiser, Andrew LaFlamme |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Embryo Nonmammalian Myosin Light Chains Myosin light-chain kinase Morpholino Protein subunit Phosphatase macromolecular substances Biology Article Animals Genetically Modified Myosin-Light-Chain Phosphatase 03 medical and health sciences Catalytic Domain Myosin Genetics Animals Phosphorylation Zebrafish 030102 biochemistry & molecular biology Gene Expression Regulation Developmental Actomyosin General Medicine biology.organism_classification Cell biology Isoenzymes Actin Cytoskeleton Alternative Splicing Protein Subunits 030104 developmental biology Myosin-light-chain phosphatase |
| Zdroj: | Gene. 675:15-26 |
| ISSN: | 0378-1119 |
| DOI: | 10.1016/j.gene.2018.06.092 |
| Popis: | Myosin phosphatase is an evolutionarily conserved regulator of actomyosin contractility, comprised of a regulatory subunit (Mypt1), and a catalytic subunit (PP1). Zebrafish has become an ideal model organism for the study of the genetic and cell physiological role of the myosin phosphatase in morphogenesis and embryonic development. We identified and characterized a novel splice variant of Mypt1 (ppp1r12a-tv202) from zebrafish, which is widely expressed during early embryonic development. Importantly, mutant alleles and antisense morpholinos that have been used to demonstrate the important role of Mypt1 in early development, not only disrupt the longer splice variants, but also tv202. The protein product of ppp1r12a-tv202 (Mypt1–202) contains the PP1-binding N-terminus, but lacks the regulatory C-terminus, which contains two highly conserved inhibitory phosphorylation sites. We observed that the protein product of tv202 assembled a constitutively active myosin phosphatase uninhibited by kinases such as Zipk. Thus, we propose that Mypt1–202 plays an important role in maintaining baseline Mlc2 dephosphorylation and actomyosin relaxation during early zebrafish development. |
| Databáze: | OpenAIRE |
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