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Originally published In Press as doi:10.1074/jbc.M005587200 on November 21, 2000

J. Biol. Chem., Vol. 276, Issue 11, 8173-8179, March 16, 2001
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Protein Kinase B beta /Akt2 Plays a Specific Role in Muscle Differentiation*

Marie VandrommeDagger §, Anne RochatDagger §, Roger Meier, Gilles CarnacDagger , Daniel Besser||, Brian A. Hemmings, Anne FernandezDagger , and Ned J. C. LambDagger **

From the Dagger  Institut de Genetique Humaine, CNRS, UPR 1142, 141 Rue de la Cardonille, 34396 Montpellier Cedex 4, France, the  Friedrich Miescher Institut, Maubeerstrasse 66, CH-4056 Basel, Switzerland, and the || Rockefeller University, Laboratory of Molecular Cell Biology, New York, New York 10021

Insulin-like growth factors positively regulate muscle differentiation through activation of the phosphatidylinositol 3-kinase/protein kinase B (PKB/Akt) signaling pathway. Here, we compare the role of the two closely related alpha  (Akt1) and beta  (Akt2) isoforms of PKB in muscle differentiation. During differentiation of C2.7 or L6D2 myoblasts, PKBbeta was up-regulated whereas expression of PKBalpha was unaltered. Although the two isoforms were found active in both myoblasts and myotubes, cell fractionation experiments indicated that they displayed distinct subcellular localizations in differentiated cells with only PKBbeta localized in the nuclei. In a transactivation assay, PKBbeta (either wild-type or constitutively active) was more efficient than PKBalpha in activating muscle-specific gene expression. Moreover, microinjection of specific antibodies to PKBbeta inhibited differentiation of muscle cells, whereas control or anti-PKBalpha antibodies did not. On the other hand, microinjection of the anti-PKBalpha antibodies caused a block in cell cycle progression in both non muscle and muscle cells, whereas anti-PKBbeta antibodies had no effect. Taken together, these results show that PKBbeta plays a crucial role in the commitment of myoblasts to differentiation that cannot be substituted by PKBalpha .

* This work was supported by grants from Association Francaise contre les Myopathies, by Association pour la Recherche contre le Cancer Grant 9484, and by Human Frontiers Science Program Organisation Collaborative Grant 533/1996-M.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ These authors contributed equally to this work.

** To whom correspondence should be addressed. Tel.: 33-499-61-99-66; Fax: 33-499-61-99-69; E-mail: ned.lamb@igh.cnrs.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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