PRAS40 regulates protein synthesis and cell cycle in C2C12 myoblasts

Molecular Medicine

Volumn 16, Issue 9-10, 2010, Pages 359-371

  Kazi, Abid A ^a   Lang, Charles H ^a  

^a PENN STATE COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CASPASE 3; DNA; INITIATION FACTOR 4E BINDING PROTEIN 1; LENTIVIRUS VECTOR; MAMMALIAN TARGET OF RAPAMYCIN; MESSENGER RNA; MYOSIN HEAVY CHAIN; PRAS40 PROTEIN; PROTEIN P21; RETINOBLASTOMA PROTEIN; SHORT HAIRPIN RNA; UNCLASSIFIED DRUG;

ANIMAL CELL; APOPTOSIS; ARTICLE; AUTOPHAGY; CELL CYCLE G1 PHASE; CELL CYCLE REGULATION; CELL CYCLE S PHASE; CELL DIFFERENTIATION; CELL PROLIFERATION; CELL SIZE; CONTROLLED STUDY; GENE EXPRESSION REGULATION; GENE SILENCING; IMMUNOBLOTTING; MOUSE; MUSCLE CELL; MYOBLAST; MYOTUBE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CLEAVAGE; PROTEIN CONTENT; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN SYNTHESIS REGULATION; PROTEIN TARGETING; RNA INTERFERENCE; UPREGULATION;

AMINOIMIDAZOLE CARBOXAMIDE; ANIMALS; APOPTOSIS; AUTOPHAGY; CELL CYCLE; CELL DIFFERENTIATION; CELL PROLIFERATION; CELL SIZE; GENE KNOCKDOWN TECHNIQUES; INSULIN-LIKE GROWTH FACTOR I; MICE; MUSCLE DEVELOPMENT; MUSCLE FIBERS, SKELETAL; MYOBLASTS; MYOSIN HEAVY CHAINS; PHOSPHOPROTEINS; PROTEIN BIOSYNTHESIS; RIBONUCLEOTIDES; RNA, SMALL INTERFERING;

EID: 77956626055     PISSN: 10761551     EISSN: None     Source Type: Journal    
DOI: 10.2119/molmed.2009.00168     Document Type: Article

References (51)

1. Kimball SR, Jefferson LS. (2006) Signaling pathways and molecular mechanisms through which branched-chain amino acids mediate translational control of protein synthesis. J. Nutr. 136 (Suppl. 1): 227S-31S.
2. Anthony JC, et al. (2002) Contribution of insulin to the translational control of protein synthesis in skeletal muscle by leucine. Am. J. Physiol. Endocrinol. Metab. 282:E1092-101.
3. Krawiec BJ, Frost RA, Vary TC, Jefferson LS, Lang CH. (2005) Hindlimb casting decreases muscle mass in part by proteasome- dependent proteolysis but independent of protein synthesis. Am. J. Physiol. Endocrinol. Metab. 289:E969-80.
4. Dunlop EA, Tee AT. (2009) Mammalian target of rapamycin complex 1: signalling inputs, substrates and feedback mechanisms. Cell Signal 21:827-35.
5. Gingras AC, Raught B, Sonenberg N. (2004) mTOR signaling to translation. Curr. Top. Microbiol. Immunol. 279:169-97.
6. Hay N, Sonenberg N. (2004) Upstream and downstream of mTOR. Genes Dev. 18:1926-45.
7. Hall MN. (2008) mTOR: what does it do? Transplant. Proc. 40 (Suppl. 10):S5-8.
8. Schmelzle T, Hall MN. (2000) TOR, a central controller of cell growth. Cell 103:253-62.
9. Balasubramanian S, et al. (2009) mTOR in growth and protection of hypertrophying myocardium. Cardiovasc. Hematol. Agents Med. Chem. 7:52-63.
10. Holz MK, Ballif BA, Gygi SP, Blenis J. (2005) mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 123:569-80.
11. Kim DH, et al. (2002) mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 110:163-75.
12. Peterson TR, et al. (2009) DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival. Cell 137:873-86.
13. Lang CH, et al. (2003) Alcohol impairs leucinemediated phosphorylation of 4E-BP1, S6K1, eIF4G, and mTOR in skeletal muscle. Am. J. Physiol. Endocrinol. Metab. 285:E1205-15.
14. Kovacina KS, et al. (2003) Identification of a proline- rich Akt substrate as a 14-3-3 binding partner. J. Biol. Chem. 278:10189-94.
15. Sancak Y, et al. (2007) PRAS40 is an insulinregulated inhibitor of the mTORC1 protein kinase. Mol. Cell. 25:903-15.
16. Wang L, Harris TE, Lawrence JC Jr. (2008) Regulation of proline-rich Akt substrate of 40 kDa (PRAS40) function by mammalian target of rapamycin complex 1 (mTORC1)-mediated phosphorylation. J. Biol. Chem. 283:15619-27.
17. Oshiro N, et al. (2007) The proline-rich Akt substrate of 40 kDa (PRAS40) is a physiological substrate of mammalian target of rapamycin complex 1. J. Biol. Chem. 282:20329-39.
18. Fonseca BD, Smith EM, Lee VH, MacKintosh C, Proud CG. (2007) PRAS40 is a target for mammalian target of rapamycin complex 1 and is required for signaling downstream of this complex. J. Biol. Chem. 282:24514-24.
19. Williamson DL, Bolster DR, Kimball SR, Jefferson LS. (2006) Time course changes in signaling pathways and protein synthesis in C2C12 myotubes following AMPK activation by AICAR. Am. J. Physiol. Endocrinol. Metab. 291:E80-9.
20. Frost RA, Lang CH, Gelato MC. (1997) Transient exposure of human myoblasts to tumor necrosis factor-alpha inhibits serum and insulin-like growth factor-I stimulated protein synthesis. Endocrinology 138:4153-9.
21. Vander Haar E, Lee SI, Bandhakavi S, Griffin TJ, Kim DH. (2007) Insulin signalling to mTOR mediated by the Akt/PKB substrate PRAS40. Nat. Cell. Biol. 9:316-23.
22. Hong-Brown LQ, Brown CR, Huber DS, Lang CH. (2007) Alcohol regulates eukaryotic elongation factor 2 phosphorylation via an AMP-activated protein kinase-dependent mechanism in C2C12 skeletal myocytes. J. Biol. Chem. 282:3702-12.
23. Giegerich R, Meyer F, Schleiermacher C. (1996) GeneFisher-software support for the detection of postulated genes. Proc. Int. Conf. Intell. Syst. Mol. Biol. 4:68-77.
24. Krawiec BJ, Nystrom GJ, Frost RA, Jefferson LS, Lang CH. (2007) AMP-activated protein kinase agonists increase mRNA content of the musclespecific ubiquitin ligases MAFbx and MuRF1 in C2C12 cells. Am. J. Physiol. Endocrinol. Metab. 292:E1555-67.
25. Lang CH, Frost RA, Vary TC. (2008) Acute alcohol intoxication increases REDD1 in skeletal muscle. Alcohol Clin. Exp. Res. 32:796-805.
26. Das A, Desai D, Pittman B, Amin S, El-Bayoumy K. (2003) Comparison of the chemopreventive efficacies of 1,4-phenylenebis(methylene)selenocyanate and selenium-enriched yeast on 4-(methylnitrosamino)- 1-(3-pyridyl)-1-butanone induced lung tumorigenesis in A/J mouse. Nutr. Cancer 46:179-85.
27. Zhivotovsky B, Nicotera P, Bellomo G, Hanson K, Orrenius S. (1993) Ca2+ and endonuclease activation in radiation-induced lymphoid cell death. Exp. Cell. Res. 207:163-70.
28. Srinivas V, Bohensky J, Shapiro IM. (2009) Autophagy: a new phase in the maturation of growth plate chondrocytes is regulated by HIF, mTOR and AMP kinase. Cells Tissues Organs 189:88-92.
29. Zeng M, Zhou JN. (2008) Roles of autophagy and mTOR signaling in neuronal differentiation of mouse neuroblastoma cells. Cell Signal 20:659-65.
30. Shaw RJ, Cantley LC. (2006) Ras, PI(3)K and mTOR signalling controls tumour cell growth. Nature 441:424-30.
31. Fingar DC, et al. (2004) mTOR controls cell cycle progression through its cell growth effectors S6K1 and 4E-BP1/eukaryotic translation initiation factor 4E. Mol. Cell. Biol. 24:200-16.
32. Fingar DC, Salama S, Tsou C, Harlow E, Blenis J. (2002) Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E. Genes. Dev. 16:1472-87.
33. Madhunapantula SV, Sharma A, Robertson GP. (2007) PRAS40 deregulates apoptosis in malignant melanoma. Cancer Res. 67:3626-36.
34. Thedieck K, et al. (2007) PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis. PLoS One 2:e1217.
35. Sartori R, et al. (2009) Smad2 and 3 transcription factors control muscle mass in adulthood. Am. J. Physiol. Cell. Physiol. 296:C1248-57.
36. Welle S, Burgess K, Thornton CA, Tawil R. (2009) Relation between extent of myostatin depletion and muscle growth in mature mice. Am. J. Physiol. Endocrinol. Metab. 297:935-40.
37. Hentges KE, et al. (2001) FRAP/mTOR is required for proliferation and patterning during embryonic development in the mouse. Proc. Natl. Acad. Sci. U. S. A. 98:13796-801.
38. Zhang LH, Lin FR. (2009) Effect of rapamycin on leukemia cell lines [in Chinese]. Zhongguo Shi Yan Xue Ye Xue Za Zhi 17:870-3.
39. Shafer A, Zhou C, Gehrig PA, Boggess JF, Bae-Jump VL. (2010) Rapamycin potentiates the effects of paclitaxel in endometrial cancer cells through inhibition of cell proliferation and induction of apoptosis. Int. J. Cancer 126:1144-54.
40. Rosner M, Fuchs C, Siegel N, Valli A, Hengstschlager M. (2009) Functional interaction of mammalian target of rapamycin complexes in regulating mammalian cell size and cell cycle. Hum. Mol. Genet. 18:3298-310.
41. Imamura K, Ogura T, Kishimoto A, Kaminishi M, Esumi H. (2001) Cell cycle regulation via p53 phosphorylation by a 5′-AMP activated protein kinase activator, 5-aminoimidazole- 4-carboxamide-1- beta-D-ribofuranoside, in a human hepatocellular carcinoma cell line. Biochem. Biophys. Res. Commun. 287:562-7.
42. Williamson DL, Butler DC, Alway SE. (2009) AMPK inhibits myoblast differentiation through a PGC-1alpha-dependent mechanism. Am. J. Physiol. Endocrinol. Metab. 297:E304-14.
43. Deng C, Zhang P, Harper JW, Elledge SJ, Leder P. (1995) Mice lacking p21CIP1/WAF1 undergo normal development, but are defective in G1 checkpoint control. Cell 82:675-84.
44. Zhang P, et al. (1999) p21(CIP1) and p57(KIP2) control muscle differentiation at the myogenin step. Genes. Dev. 13:213-24.
45. Hawke TJ, et al. (2003) p21 is essential for normal myogenic progenitor cell function in regenerating skeletal muscle. Am. J. Physiol. Cell. Physiol. 285:C1019-27.
46. Lee YJ, et al. (2009) Involvement of a p53- independent and post-transcriptional upregulation for p21WAF/CIP1 following destabilization of the actin cytoskeleton. Int. J. Oncol. 34:581-9.
47. Parker SB, et al. (1995) p53-independent expression of p21Cip1 in muscle and other terminally differentiating cells. Science 267:1024-7.
48. Mammucari C, Schiaffino S, Sandri M. (2008) Downstream of Akt: FoxO3 and mTOR in the regulation of autophagy in skeletal muscle. Autophagy 4:524-6.
49. Annovazzi L, et al. (2009) mTOR, S6 and AKT expression in relation to proliferation and apoptosis/ autophagy in glioma. Anticancer Res. 29:3087-94.
50. Jung CH, Ro SH, Cao J, Otto NM, Kim DH. (2010) mTOR regulation of autophagy. FEBS Lett. 584:1287-95.
51. Ravikumar B, et al. (2004) Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat. Genet. 36:585-95.