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Pkn Is a novel partner of cyclin T2a in muscle differentiation
Author(s) -
Cottone Giuliano,
Baldi Alfonso,
Palescandolo Emanuele,
Manente Lucrezia,
Penta Roberta,
Paggi Marco G.,
De Luca Antonio
Publication year - 2006
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.20566
Subject(s) - microbiology and biotechnology , cyclin , chemistry , biology , cell , cell cycle , biochemistry
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. J. Cell. Physiol. 207: 232–237, 2006. © 2005 Wiley‐Liss, Inc.