- About this Journal ·
- Abstracting and Indexing ·
- Advance Access ·
- Aims and Scope ·
- Annual Issues ·
- Article Processing Charges ·
- Articles in Press ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
Journal of Biomedicine and Biotechnology
Volume 2012 (2012), Article ID 989263, 8 pages
Localization and Regulation of the N Terminal Splice Variant of PGC-1α in Adult Skeletal Muscle Fibers
Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201-1503, USA
Received 23 September 2011; Accepted 26 October 2011
Academic Editor: Aikaterini Kontrogianni-Konstantopoulos
Copyright © 2012 Tiansheng Shen et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- P. Puigserver, Z. Wu, C. W. Park, R. Graves, M. Wright, and B. M. Spiegelman, “A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis,” Cell, vol. 92, no. 6, pp. 829–839, 1998.
- J. Lin, H. Wu, P. T. Tarr et al., “Transcriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres,” Nature, vol. 418, no. 6899, pp. 797–801, 2002.
- Z. Wu, P. Puigserver, U. Andersson et al., “Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1,” Cell, vol. 98, no. 1, pp. 115–124, 1999.
- O. H. Mortensen, L. Frandsen, P. Schjerling, E. Nishimura, and N. Grunnet, “PGC-1α and PGC-1β have both similar and distinct effects on myofiber switching toward an oxidative phenotype,” American Journal of Physiology, Endocrinology and Metabolism, vol. 291, no. 4, pp. E807–E816, 2006.
- A. S. Mathai, A. Bonen, C. R. Benton, D. L. Robinson, and T. E. Graham, “Rapid exercise-induced changes in PGC-1α mRNA and protein in human skeletal muscle,” Journal of Applied Physiology, vol. 105, no. 4, pp. 1098–1105, 2008.
- S. Terada and I. Tabata, “Effects of acute bouts of running and swimming exercise on PGC-1α protein expression in rat epitrochlearis and soleus muscle,” American Journal of Physiology, Endocrinology and Metabolism, vol. 286, no. 2, pp. E208–E216, 2004.
- D. Knutti, D. Kressler, and A. Kralli, “Regulation of the transcriptional coactivator PGC-1 via MAPK-sensitive interaction with a repressor,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 17, pp. 9713–9718, 2001.
- P. Puigserver, J. Rhee, J. Lin et al., “Cytokine stimulation of energy expenditure through p38 MAP kinase activation of PPARγ coactivator-1,” Molecular Cell, vol. 8, no. 5, pp. 971–982, 2001.
- Z. Yan, P. Li, and T. Akimoto, “Transcriptional control of the Pgc-1α gene in skeletal muscle in vivo,” Exercise and Sport Sciences Reviews, vol. 35, no. 3, pp. 97–101, 2007.
- I. Irrcher, P. J. Adhihetty, T. Sheehan, A. M. Joseph, and D. A. Hood, “PPARγ coactivator-1α expression during thyroid hormone- and contractile activity-induced mitochondrial adaptations,” American Journal of Physiology—Cell Physiology, vol. 284, no. 6, pp. C1669–C1677, 2003.
- S. Jäer, C. Handschin, J. St-Pierre, and B. M. Spiegelman, “AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 29, pp. 12017–12022, 2007.
- Y. Zhang, P. Huypens, A. W. Adamson et al., “Alternative mRNA splicing produces a novel biologically active short isoform of PGC-1α,” Journal of Biological Chemistry, vol. 284, no. 47, pp. 32813–32826, 2009.
- J. S. Chang, P. Huypens, Y. Zhang, A. Kralli, and T. W. Gettys, “Regulation of NT-PGC-1α subcellular localization and function by protein kinase A-dependent modulation of nuclear export by CRM1,” Journal of Biological Chemistry, vol. 285, no. 23, pp. 18039–18050, 2010.
- J. Trausch-Azar, T. C. Leone, D. P. Kelly, and A. L. Schwartz, “Ubiquitin proteasome-dependent degradation of the transcriptional coactivator PGC-1α via the N-terminal pathway,” Journal of Biological Chemistry, vol. 285, no. 51, pp. 40192–40200, 2010.
- Y. Liu, S. L. Carroll, M. G. Klein, and M. F. Schneider, “Calcium transients and calcium homeostasis in adult mouse fast-twitch skeletal muscle fibers in culture,” American Journal of Physiology—Cell Physiology, vol. 272, no. 6, pp. C1919–C1927, 1997.
- Y. Liu, Z. Cseresnyés, W. R. Randall, and M. F. Schneider, “Activity-dependent nuclear translocation and intranuclear distribution of NFATc in adult skeletal muscle fibers,” Journal of Cell Biology, vol. 155, no. 1, pp. 27–39, 2001.
- T. Shen, Y. Liu, M. Contreras, E. O. Hernández-Ochoa, W. R. Randall, and M. F. Schneider, “DNA binding sites target nuclear NFATc1 to heterochromatin regions in adult skeletal muscle fibers,” Histochemistry and Cell Biology, vol. 134, no. 4, pp. 387–402, 2010.
- T. Shen, Y. Liu, Z. Cseresnyés, A. Hawkins, W. R. Randall, and M. F. Schneider, “Activity- and calcineurin-independent nuclear shuttling of NFATc1, but Not NFATc3, in adult skeletal muscle fibers,” Molecular Biology of the Cell, vol. 17, no. 4, pp. 1570–1582, 2006.
- Y. Liu, W. R. Randall, and M. F. Schneider, “Activity-dependent and -independent nuclear fluxes of HDAC4 mediated by different kinases in adult skeletal muscle,” Journal of Cell Biology, vol. 168, no. 6, pp. 887–897, 2005.
- R. C. Ho, N. Fujii, L. A. Witters, M. F. Hirshman, and L. J. Goodyear, “Dissociation of AMP-activated protein kinase and p38 mitogen-activated protein kinase signaling in skeletal muscle,” Biochemical and Biophysical Research Communications, vol. 362, no. 2, pp. 354–359, 2007.
- E. Saijou, T. Itoh, K. W. Kim, S. I. Iemura, T. Natsume, and A. Miyajima, “Nucleocytoplasmic shuttling of the zinc finger protein EZI is mediated by importin-7-dependent nuclear import and CRM1-independent export mechanisms,” Journal of Biological Chemistry, vol. 282, no. 44, pp. 32327–32337, 2007.