Pkn is a novel partner of cyclin T2a in muscle differentiation

Giuliano Cottone, Alfonso Baldi, Emanuele Palescandolo, Lucrezia Manente, Roberta Penta, Marco G. Paggi, Antonio De Luca

Research output: Contribution to journalArticlepeer-review


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 PKNα, 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 PKNα 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 PKNα 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 PKNα as a novel partner of Cyclin T2a in this process.

Original languageEnglish
Pages (from-to)232-237
Number of pages6
JournalJournal of Cellular Physiology
Issue number1
Publication statusPublished - Apr 2006

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Cell Biology
  • Physiology


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