Organization of the genetic locus for chicken myosin light chain kinase is complex: Multiple proteins are encoded and exhibit differential expression and localization

Konstantin G. Birukov, James P. Schavocky, Vladimir P. Shirinsky, Margarita V. Chibalina, Linda J. Van Eldik, D. Martin Watterson

Research output: Contribution to journalArticlepeer-review

50 Scopus citations

Abstract

We report that the genetic locus that encodes vertebrate smooth muscle and nonmuscle myosin light chain kinase (MLCK) and kinase-related protein (KRP) has a complex arrangement and a complex pattern of expression. Three proteins are encoded by 31 exons that have only one variation, that of the first exon of KRP, and the genomic locus spans approximately 100 kb of DNA. The three proteins can differ in their relative abundance and localization among tissues and with development. MLCK is a calmodulin (CAM) regulated protein kinase that phosphorylates the light chain of myosin II. The chicken has two MLCK isoforms encoded by the MLCK/KRP locus. KRP does not bind CaM and is not a protein kinase. However, KRP binds to and regulates the structure of myosin II. Thus, KRP and MLCK have the same subcellular target, the myosin II molecular motor system. We examined the tissue and cellular localization of KRP and MLCK in the chicken embryo and in adult chicken tissues. We report on the selective localization of KRP and MLCK among and within tissues and on a differential distribution of the proteins between embryonic and adult tissues. The results fill a void in our knowledge about the organization of the MLCK/KRP genetic locus, which appears to be a late evolving regulatory paradigm, and suggest an independent and complex regulation of expression of the gene products from the MLCK/KRP genetic locus that may reflect a basic principle found in other eukaryotic gene clusters that encode functionally linked proteins.

Original languageEnglish
Pages (from-to)402-413
Number of pages12
JournalJournal of Cellular Biochemistry
Volume70
Issue number3
DOIs
StatePublished - Sep 1 1998

Funding

FundersFunder number
National Institute of General Medical SciencesR01GM030861

    Keywords

    • Calcium
    • Calmodulin
    • Development
    • Genome
    • Heart
    • Immunohistochemistry
    • Protein kinase
    • Signal transduction
    • Smooth muscle
    • Tissue selective

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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