PUBLICATION
Orthologous relationship of obscurin and Unc-89: phylogeny of a novel family of tandem myosin light chain kinases
- Authors
- Sutter, S.B., Raeker, M.O., Borisov, A.B., and Russell, M.W.
- ID
- ZDB-PUB-040609-1
- Date
- 2004
- Source
- Development genes and evolution 214(7): 352-359 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Base Sequence
- Caenorhabditis elegans Proteins/genetics*
- Cluster Analysis
- DNA Primers
- Evolution, Molecular
- Gene Components
- Gene Duplication
- Guanine Nucleotide Exchange Factors/genetics*
- Humans
- Invertebrates/genetics*
- Molecular Sequence Data
- Multigene Family/genetics
- Muscle Proteins/genetics*
- Myofibrils/metabolism
- Myosin-Light-Chain Kinase/genetics*
- Phylogeny*
- Rho Guanine Nucleotide Exchange Factors
- Sequence Alignment
- Sequence Analysis, DNA
- Vertebrates/genetics*
- Zebrafish Proteins/genetics*
- PubMed
- 15185077 Full text @ Dev. Genes Evol.
Citation
Sutter, S.B., Raeker, M.O., Borisov, A.B., and Russell, M.W. (2004) Orthologous relationship of obscurin and Unc-89: phylogeny of a novel family of tandem myosin light chain kinases. Development genes and evolution. 214(7):352-359.
Abstract
Myosin light chain kinases (MLCK) are a family of signaling proteins that are required for cytoskeletal remodeling in myocytes. Recently, two novel MLCK proteins, SPEG and obscurin-MLCK, were identified with the unique feature of two tandemly-arranged MLCK domains. In this study, the evolutionary origins of this MLCK subfamily were traced to a probable orthologue of obscurin-MLCK in Drosophila melanogaster, Drosophila Unc-89, and the MLCK kinase domains of zebrafish SPEG, zebrafish obscurin-MLCK, and human SPEG were characterized. Phylogenetic analysis of the MLCK domains indicates that the carboxy terminal kinase domains of obscurin-MLCK, SPEG and Unc-89 are more closely related to each other than to the amino terminal kinase domains or to other MLCKs, supporting the assertion that obscurin-MLCK is the vertebrate orthologue of Caenorhabditis elegans Unc-89, a giant multidomain protein that is required for normal myofibril assembly. The apparent lack of an invertebrate orthologue of SPEG and the conserved exon structure of the kinase domains between SPEG and obscurin-MLCK suggests that SPEG arose from obscurin-MLCK by a gene duplication event. The length of the primary amino acid sequence between the immunoglobulin (Ig) domains associated with the MLCK motifs is conserved in obscurin-MLCK, SPEG and C. elegans Unc-89, suggesting that these putative protein interaction domains may target the kinases to highly conserved intracellular sites. The conserved arrangement of the tandem MLCK domains and their relatively restricted expression in striated muscle indicates that further characterization of this novel MLCK subfamily may yield important insights into cardiac and skeletal muscle physiology.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping