Characterization of Osterix Protein Stability and Physiological Role in Osteoblast Differentiation

PLoS ONE

Volumn 8, Issue 2, 2013, Pages

  Peng, Yanyan ^a   Shi, Kaikai ^a   Wang, Lintao ^a   Lu, Jianlei ^a   Li, Hongwei ^a   Pan, Shiyang ^b,c   Ma, Changyan ^a  

^a NANJING MEDICAL UNIVERSITY   (China)

^b THE FIRST AFFILIATED HOSPITAL OF NANJING MEDICAL UNIVERSITY   (China)

^c National Key Clinical Department of Laboratory Medicine   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; COLLAGEN TYPE 1; CYCLOHEXIMIDE; LACTACYSTIN; LUCIFERASE; LYSINE; OSTEOCALCIN; PROTEASOME; TRANSCRIPTION FACTOR OSTERIX; UBIQUITIN;

ARTICLE; CELL DIFFERENTIATION; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; MAMMAL CELL; OSTEOBLAST; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN PROCESSING; PROTEIN STABILITY; REGULATORY MECHANISM; SIGNAL TRANSDUCTION; UBIQUITINATION;

ALKALINE PHOSPHATASE; BINDING SITES; BONE AND BONES; CALCIFICATION, PHYSIOLOGIC; CELL DIFFERENTIATION; CELL LINE; GENE EXPRESSION REGULATION; GENETIC MARKERS; HUMANS; MUTAGENESIS, SITE-DIRECTED; MUTATION; OSTEOBLASTS; PROTEASOME INHIBITORS; PROTEIN STABILITY; PROTEOLYSIS; RNA, MESSENGER; TRANSCRIPTION FACTORS; UBIQUITINATION;

EID: 84874096115     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0056451     Document Type: Article

References (29)

1. Katagiri T, Takahashi N, (2002) Regulatory mechanisms of osteoblast and osteoclast differentiation. Oral Dis 8: 147-159.
2. Kawamura N, Kugimiya F, Oshima Y, Ohba S, Ikeda T, et al. (2007) Akt1 in osteoblasts and osteoclasts controls bone remodeling. PLoS One 2(10): e1058.
3. Heino TJ, Hentunen TA, (2008) Differentiation of osteoblasts and osteocytes from mesenchymal stem cells. Curr Stem Cell Res Ther 3: 131-145.
4. Zhang C, (2010) Transcriptional regulation of bone formation by the osteoblast-specific transcription factor Osx. J Orthop Surg Res 5: 37.
5. Nakashima K, Zhou X, Kunkel G, Zhang Z, Deng JM, et al. (2002) The novel zinc finger-containing transcription factor osterix is required for osteoblast differentiation and bone formation. Cell 108: 17-29.
6. Zhou X, Zhang Z, Feng JQ, Dusevich VM, Sinha K, et al. (2010) Multiple functions of Osterix are required for bone growth and homeostasis in postnatal mice. Proc Natl Acad Sci USA 107: 12919-12924.
7. Baek WY, de Crombrugghe B, Kim JE, (2010) Postnatally induced inactivation of Osterix in osteoblasts results in the reduction of bone formation and maintenance. Bone 46: 920-928.
8. Baek WY, Lee MA, Jung JW, Kim SY, Akiyama H, et al. (2009) Positive regulation of adult bone formation by osteoblast-specific transcription factor osterix. J Bone Miner Res 24: 1055-1065.
9. Matsubara T, Kida K, Yamaguchi A, Hata K, Ichida F, et al. (2008) BMP2 regulates Osterix through Msx2 and Runx2 during osteoblast differentiation. J Biol Chem 283: 29119-29125.
10. Lee MH, Kwon TG, Park HS, Wozney JM, Ryoo HM, (2003) BMP-2-induced Osterix expression is mediated by Dlx5 but is independent of Runx2. Biochem Biophys Res Commun 309: 689-694.
11. Voutsadakis IA, (2012) The ubiquitin-proteasome system and signal transduction pathways regulating Epithelial Mesenchymal transition of cancer. J Biomed Sci 19: 67.
12. Ciechanover A, (2005) Proteolysis: from the lysosome to ubiquitin and the proteasome. Nat Rev Mol Cell Biol 6: 79-87.
13. Glickman MH, Ciechanover A, (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82: 373-428.
14. Varshavsky A, (2005) Regulated protein degradation. Trends Biochem Sci 30: 283-286.
15. Kim MY, Bae JS, Kim TH, Park JM, Ahn YH, (2012) Role of transcription factor modifications in the pathogenesis of insulin resistance. Exp Diabetes Res 2012: 716425.
16. Sorokin AV, Kim ER, Ovchinnikov LP, (2009) Proteasome system of protein degradation and processing. Biochemistry (Mosc) 74: 1411-1442.
17. Rock KL, Gramm C, Rothstein L, Clark K, Stein R, et al. (1994) Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78: 761-771.
18. Craiu A, Gaczynska M, Akopian T, Gramm CF, Fenteany G, et al. (1997) Lactacystin and clasto-lactacystin beta-lactone modify multiple proteasome beta-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation. J Biol Chem 272: 13437-13445.
19. Mayer RJ, Ciechanover A, Rechsteiner M (2005) Protein Degradation Handbook: Weinheim, Germany: Wiley-VCH.
20. Mayer RJ, Ciechanover A, Rechsteiner M (2006) Protein Degradation Handbook: Weinheim, Germany: Wiley-VCH.
21. Mayer RJ, Ciechanover A, Rechsteiner M (2008) Protein Degradation Handbook: Weinheim, Germany: Wiley-VCH.
22. Weissman AM, (2001) Themes and variations on ubiquitylation. Nat Rev Mol Cell Biol 2: 169-178.
23. Hobler SC, Wang JJ, Williams AB, Melandri F, Sun X, et al. (1999) Sepsis is associated with increased ubiquitinconjugating enzyme E214k mRNA in skeletal muscle. Am J Physiol 276: R468-473.
24. Shi Y, Xu P, Qin J, (2011) Ubiquitinated proteome: ready for global? Mol Cell Proteomics 10(5): R110.006882.
25. Cai Q, Robertson ES (2010) Ubiquitin/SUMO modification regulates VHL protein stability and nucleocytoplasmic localization. PLoS One 5(9): doi:pii: e12636.
26. Katagiri T, Yamaguchi A, Komaki M, Abe E, Takahashi N, et al. (1994) Bone morphogenetic protein-2 converts the differentiation pathway of C2C12 myoblasts into the osteoblast lineage. J Cell Biol 127: 1755-1766.
27. Sasaki A, Masuda Y, Iwai K, Ikeda K, Watanabe K, (2002) A RING finger protein Praja1 regulates Dlx5-dependent transcription through its ubiquitin ligase activity for the Dlx/Msx-interacting MAGE/Necdin family protein, Dlxin-1. J Biol Chem 277: 22541-22546.
28. Garrett IR, Chen D, Gutierrez G, Zhao M, Escobedo A, et al. (2003) Selective inhibitors of the osteoblast proteasome stimulate bone formation in vivo and in vitro. J Clin Invest 111: 1771-1782.
29. Zhao X, Chao Y, Chen P, Liu D, Su P, et al. (2012) hRpn13, a newly identified component of the 19S particle, regulates proliferation, differentiation, and function in the human osteoblast-like cell line MG63. [corrected]. J Physiol Biochem 68: 129-139.