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

Article Details


Cottone G, Baldi A, Palescandolo E, Manente L, Penta R, Paggi MG, De Luca A

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

J Cell Physiol. 2006 Apr;207(1):232-7. doi: 10.1002/jcp.20566.

PubMed ID
16331689 [ View in PubMed

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.

DrugBank Data that Cites this Article

NameUniProt ID
Serine/threonine-protein kinase N1Q16512Details