Pkn is a novel partner of cyclin T2a in muscle differentiation.

With the aim to find novel partners of human Cyclin T2a, we performed a two-hybrid screening in yeast using the full-length cDNA of this cyclin as bait, and a human heart cDNA library as preys source. Upon several interesting genes selected, our attention has been focused on the cDNA coding ...
for PKNalpha, a fatty acid- and Rho-activated serine/threonine protein kinase, having a catalytic domain homologous to protein kinase C family. Co-immunoprecipitation and in vitro pull-down assays independently confirmed the interaction between the two proteins. Luciferase assays, performed on NIH3T3 cell extracts after transfection with a MyoD-responsive promoter, pointed out that PKNalpha was able to enhance MyoD-dependent transcription, and that this effect was further increased when cyclin T2a was co-overexpressed. Finally, overexpression of both Cyclin T2a and PKNalpha in C2C12 cells strongly enhanced the expression of myogenic differentiation markers, such as Myogenin and Myosin Heavy Chain, during starvation-induced differentiation. Taken together, our data strengthen the hypothesis that Cyclin T2a plays a role in muscle differentiation, and propose PKNalpha as a novel partner of Cyclin T2a in this process.
Mesh Terms:
Animals, Binding Sites, Binding, Competitive, Cell Differentiation, Cell Line, Cyclin T, Cyclin-Dependent Kinase 9, Cyclins, DNA, Complementary, Gene Expression, Humans, Mice, Muscle Cells, Mutation, MyoD Protein, Myogenin, Myosin Heavy Chains, NIH 3T3 Cells, Plasmids, Protein Binding, Protein Kinase C, Protein-Serine-Threonine Kinases, Protein-Tyrosine Kinases, Recombinant Proteins, Saccharomyces cerevisiae, Transfection, Two-Hybrid System Techniques
J. Cell. Physiol.
Date: Apr. 01, 2006
Download Curated Data For This Publication
149338
Switch View:
  • Interactions 4