PUBLICATION
Alternative splicing of (ppp1r12a/mypt1) in zebrafish produces a novel myosin phosphatase targeting subunit
- Authors
- LaFlamme, A., Young, K.E., Lang, I., Weiser, D.C.
- ID
- ZDB-PUB-180701-9
- Date
- 2018
- Source
- Gene 675: 15-26 (Journal)
- Registered Authors
- Weiser, Douglas C.
- Keywords
- Actomyosin, Convergent extension, Gastrulation, Myosin phosphatase, Mypt1, PP1, Splicing, Zebrafish
- MeSH Terms
-
- Actin Cytoskeleton/metabolism
- Actomyosin/genetics
- Actomyosin/metabolism
- Alternative Splicing/genetics*
- Animals
- Animals, Genetically Modified
- Catalytic Domain/genetics
- Embryo, Nonmammalian
- Gene Expression Regulation, Developmental
- Isoenzymes/chemistry
- Isoenzymes/genetics
- Myosin Light Chains/metabolism
- Myosin-Light-Chain Phosphatase/chemistry*
- Myosin-Light-Chain Phosphatase/genetics*
- Myosin-Light-Chain Phosphatase/metabolism
- Phosphorylation
- Protein Subunits/chemistry
- Protein Subunits/genetics
- Zebrafish/embryology
- Zebrafish/genetics*
- PubMed
- 29960069 Full text @ Gene
Citation
LaFlamme, A., Young, K.E., Lang, I., Weiser, D.C. (2018) Alternative splicing of (ppp1r12a/mypt1) in zebrafish produces a novel myosin phosphatase targeting subunit. Gene. 675:15-26.
Abstract
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping