JunB transcription factor maintains skeletal muscle mass and promotes hypertrophy

Decreasing JunB expression causes muscle atrophy, whereas overexpression induces hypertrophy and blocks atrophy via myostatin inhibition and regulation of atrogin-1 and MuRF expression via FoxO3.

[1]  A. Goldberg,et al.  Increase in ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and atrophy denervation. , 1995, The Biochemical journal.

[2]  T. Lømo,et al.  Calcineurin controls nerve activity-dependent specification of slow skeletal muscle fibers but not muscle growth , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[3]  A. Goldberg,et al.  Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy. , 1990, The Journal of biological chemistry.

[4]  A. Brunet,et al.  The FoxO code , 2008, Oncogene.

[5]  Devjit Tripathy,et al.  Effect of acute physiological hyperinsulinemia on gene expression in human skeletal muscle in vivo. , 2008, American journal of physiology. Endocrinology and metabolism.

[6]  G. Yancopoulos,et al.  The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. , 2004, Molecular cell.

[7]  A. Goldberg,et al.  Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[8]  E. Bossy‐Wetzel,et al.  Cell cycle‐dependent variations in c‐Jun and JunB phosphorylation: a role in the control of cyclin D1 expression , 2000, The EMBO journal.

[9]  Jiandie D. Lin,et al.  PGC-1α protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription , 2006, Proceedings of the National Academy of Sciences.

[10]  D. Allen,et al.  Regulation of myostatin expression and myoblast differentiation by FoxO and SMAD transcription factors. , 2006, American journal of physiology. Cell physiology.

[11]  A. Goldberg,et al.  FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. , 2007, Cell metabolism.

[12]  D J Glass,et al.  Identification of Ubiquitin Ligases Required for Skeletal Muscle Atrophy , 2001, Science.

[13]  R. Schwartz,et al.  The vascular smooth muscle alpha-actin gene is reactivated during cardiac hypertrophy provoked by load. , 1991, The Journal of clinical investigation.

[14]  Michael E. Greenberg,et al.  c-Jun dimerizes with itself and with c-Fos, forming complexes of different DNA binding affinities , 1988, Cell.

[15]  B. Franza,et al.  Fos and jun: The AP-1 connection , 1988, Cell.

[16]  E. Wagner,et al.  AP-1 – Introductory remarks , 2001, Oncogene.

[17]  W. Dayton,et al.  Effect of sera from fed and fasted pigs on proliferation and protein turnover in cultured myogenic cells. , 1988, Journal of animal science.

[18]  Ugo Carraro,et al.  Functional in vivo gene transfer into the myofibers of adult skeletal muscle. , 2003, Biochemical and biophysical research communications.

[19]  G. Yancopoulos,et al.  Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo , 2001, Nature Cell Biology.

[20]  A. Goldberg,et al.  FoxO3 controls autophagy in skeletal muscle in vivo. , 2007, Cell metabolism.

[21]  A. Goldberg,et al.  Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy. , 1995, The Biochemical journal.

[22]  C. Mammucari,et al.  Smad2 and 3 transcription factors control muscle mass in adulthood. , 2009, American journal of physiology. Cell physiology.

[23]  M. Matsui,et al.  In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. , 2003, Molecular biology of the cell.

[24]  Marco Sandri,et al.  Foxo Transcription Factors Induce the Atrophy-Related Ubiquitin Ligase Atrogin-1 and Cause Skeletal Muscle Atrophy , 2004, Cell.

[25]  D. Glass,et al.  Skeletal muscle hypertrophy and atrophy signaling pathways. , 2005, The international journal of biochemistry & cell biology.

[26]  E. Olson,et al.  Different members of the jun proto-oncogene family exhibit distinct patterns of expression in response to type beta transforming growth factor. , 1990, The Journal of biological chemistry.

[27]  W. Aird,et al.  The Akt-regulated Forkhead Transcription Factor FOXO3a Controls Endothelial Cell Viability through Modulation of the Caspase-8 Inhibitor FLIP* , 2004, Journal of Biological Chemistry.

[28]  M. Karin,et al.  Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated trans-acting factor , 1987, Cell.

[29]  E. Wagner,et al.  JunB suppresses cell proliferation by transcriptional activation of p16INK4a expression , 2000, The EMBO journal.

[30]  A. Goldberg,et al.  What do we really know about the ubiquitin-proteasome pathway in muscle atrophy? , 2001, Current opinion in clinical nutrition and metabolic care.

[31]  S. Hatakeyama,et al.  Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size. , 2009, American journal of physiology. Cell physiology.

[32]  Lung Yu,et al.  Systemic treatment with protein synthesis inhibitors attenuates the expression of cocaine memory , 2010, Behavioural Brain Research.

[33]  A. Goldberg,et al.  Patterns of gene expression in atrophying skeletal muscles: response to food deprivation , 2002, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[34]  W. Schaper,et al.  Proto-oncogene expression in porcine myocardium subjected to ischemia and reperfusion. , 1992, Circulation research.

[35]  T. Hunter,et al.  Oncogene jun encodes a sequence-specific trans- activator similar to AP-1 , 1988, Nature.

[36]  Yukio Yoneda,et al.  A tale of early response genes. , 2004, Biological & pharmaceutical bulletin.

[37]  Luca Scorrano,et al.  Mitochondrial fission and remodelling contributes to muscle atrophy , 2010, The EMBO journal.

[38]  S. Kandarian,et al.  Intracellular signaling during skeletal muscle atrophy , 2006, Muscle & nerve.

[39]  A. Goldberg,et al.  Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases , 2007, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[40]  A. Goldberg,et al.  The role of increased proteolysis in the atrophy and arrest of proliferation in serum‐deprived fibroblasts , 1984, Journal of cellular physiology.

[41]  A. Goldberg,et al.  IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1. , 2004, American journal of physiology. Endocrinology and metabolism.

[42]  A. Goldberg,et al.  Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression , 2004, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[43]  A. Goldberg,et al.  Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway. , 1996, The New England journal of medicine.

[44]  A. Clerk,et al.  Glycogen synthase kinases 3α and 3β in cardiac myocytes: regulation and consequences of their inhibition , 2008 .

[45]  R. Scarpulla,et al.  Electrical stimulation of neonatal cardiomyocytes results in the sequential activation of nuclear genes governing mitochondrial proliferation and differentiation. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[46]  M. Yaniv,et al.  Jun DNA-binding is modulated by mutations between the leucines or by direct interaction of fos with the TGACTCA sequence. , 1989, The New biologist.

[47]  P. Coffer,et al.  FOXO-binding partners: it takes two to tango , 2008, Oncogene.

[48]  A. Clerk,et al.  Glycogen synthase kinases 3alpha and 3beta in cardiac myocytes: regulation and consequences of their inhibition. , 2008, Cellular signalling.

[49]  D. Cameron-Smith,et al.  STAT3 signaling is activated in human skeletal muscle following acute resistance exercise. , 2007, Journal of applied physiology.

[50]  J. L. Rosa,et al.  JunB Is Involved in the Inhibition of Myogenic Differentiation by Bone Morphogenetic Protein-2* , 1998, The Journal of Biological Chemistry.

[51]  C. Rommel,et al.  Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways , 2001, Nature Cell Biology.