메뉴 건너뛰기




Volumn 4, Issue 1, 2013, Pages

E3 ubiquitin ligase-mediated regulation of bone formation and tumorigenesis

Author keywords

bone tumors; Cbl proteins; proteasome; receptor tyrosine kinases; ubiquitin ligases; ubiquitination

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; BETA CATENIN; BONE MORPHOGENETIC PROTEIN 2; BORTEZOMIB; CBL PROTEIN; COLONY STIMULATING FACTOR 1; EPIDERMAL GROWTH FACTOR RECEPTOR; FIBROBLAST GROWTH FACTOR RECEPTOR; FIBROBLAST GROWTH FACTOR RECEPTOR 2; GLYCOGEN SYNTHASE KINASE 3BETA; INSULIN RECEPTOR SUBSTRATE 1; PENTAPEPTIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PLATELET DERIVED GROWTH FACTOR RECEPTOR; PROTEASOME INHIBITOR; PROTEIN KINASE B; PROTEIN TYROSINE KINASE; RECEPTOR ACTIVATOR OF NUCLEAR FACTOR KAPPA B; SOMATOMEDIN RECEPTOR; STAT5 PROTEIN; TRANSCRIPTION FACTOR GLI2; TRANSCRIPTION FACTOR RUNX2; TUMOR NECROSIS FACTOR ALPHA; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN PROTEIN LIGASE;

EID: 84872202144     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2012.217     Document Type: Review
Times cited : (73)

References (139)
  • 1
    • 23944474593 scopus 로고    scopus 로고
    • Intracellular protein degradation: From a vague idea, through the lysosome and the ubiquitin-proteasome system, and onto human diseases and drug targeting
    • Ciechanover A. Intracellular protein degradation: from a vague idea, through the lysosome and the ubiquitin-proteasome system, and onto human diseases and drug targeting. Cell Death Differ 2005; 12: 1178-1190.
    • (2005) Cell Death Differ , vol.12 , pp. 1178-1190
    • Ciechanover, A.1
  • 2
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination
    • Komander D. The emerging complexity of protein ubiquitination. Biochem Soc Trans 2009; 37(Pt 5): 937-953.
    • (2009) Biochem Soc Trans , vol.37 , Issue.PART 5 , pp. 937-953
    • Komander, D.1
  • 3
    • 70349441058 scopus 로고    scopus 로고
    • Ubiquitin-binding domains - From structures to functions
    • Dikic I, Wakatsuki S, Walters KJ. Ubiquitin-binding domains - from structures to functions. Nat Rev Mol Cell Biol 2009; 10: 659-671.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 659-671
    • Dikic, I.1    Wakatsuki, S.2    Walters, K.J.3
  • 4
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander D, Clague MJ, Urbe S. Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol 2009; 10: 550-563.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 5
    • 33644515991 scopus 로고    scopus 로고
    • The ubiquitin proteolytic system: From an idea to the patient bed
    • Ciechanover A. The ubiquitin proteolytic system: from an idea to the patient bed. Proc Am Thorac Soc 2006; 3: 21-31.
    • (2006) Proc Am Thorac Soc , vol.3 , pp. 21-31
    • Ciechanover, A.1
  • 6
    • 84858123174 scopus 로고    scopus 로고
    • Ubiquitin ligases and beyond
    • Dikic I, Robertson M. Ubiquitin ligases and beyond. BMC Biol 2012; 10: 22.
    • (2012) BMC Biol , vol.10 , pp. 22
    • Dikic, I.1    Robertson, M.2
  • 7
    • 84861783400 scopus 로고    scopus 로고
    • Ubiquitin-binding proteins: Decoders of ubiquitin-mediated cellular functions
    • Husnjak K, Dikic I. Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions. Annu Rev Biochem 2012; 81: 291-322.
    • (2012) Annu Rev Biochem , vol.81 , pp. 291-322
    • Husnjak, K.1    Dikic, I.2
  • 8
    • 80051733972 scopus 로고    scopus 로고
    • Ubiquitination of e3 ligases: Self-regulation of the ubiquitin system via proteolytic and non-proteolytic mechanisms
    • de Bie P, Ciechanover A. Ubiquitination of E3 ligases: self-regulation of the ubiquitin system via proteolytic and non-proteolytic mechanisms. Cell Death Differ 2011; 18: 1393-1402.
    • (2011) Cell Death Differ , vol.18 , pp. 1393-1402
    • De Bie, P.1    Ciechanover, A.2
  • 9
    • 79953667762 scopus 로고    scopus 로고
    • Advances in osteoclast biology: Old findings and new insights from mouse models
    • Edwards JR, Mundy GR. Advances in osteoclast biology: old findings and new insights from mouse models. Nat Rev Rheumatol 2011; 7: 235-243.
    • (2011) Nat Rev Rheumatol , vol.7 , pp. 235-243
    • Edwards, J.R.1    Mundy, G.R.2
  • 10
    • 0037673933 scopus 로고    scopus 로고
    • Control of osteoblast function and regulation of bone mass
    • DOI 10.1038/nature01660
    • Harada S, Rodan GA. Control of osteoblast function and regulation of bone mass. Nature 2003; 423: 349-355. (Pubitemid 40852710)
    • (2003) Nature , vol.423 , Issue.6937 , pp. 349-355
    • Harada, S.-I.1    Rodan, G.A.2
  • 12
    • 42749092987 scopus 로고    scopus 로고
    • Transcription factors controlling osteoblastogenesis
    • Marie PJ. Transcription factors controlling osteoblastogenesis. Arch Biochem Biophys 2008; 473: 98-105.
    • (2008) Arch Biochem Biophys , vol.473 , pp. 98-105
    • Marie, P.J.1
  • 13
    • 0034455103 scopus 로고    scopus 로고
    • Birth and death of bone cells: Basic regulatory mechanisms and implications for the pathogenesis and treatment of osteoporosis
    • DOI 10.1210/er.21.2.115
    • Manolagas SC. Birth and death of bone cells: basic regulatory mechanisms and implications for the pathogenesis and treatment of osteoporosis. Endocr Rev 2000; 21: 115-137. (Pubitemid 32275592)
    • (2000) Endocrine Reviews , vol.21 , Issue.2 , pp. 115-137
    • Manolagas, S.C.1
  • 14
    • 0344276470 scopus 로고    scopus 로고
    • Runx2/Cbfa1: A multifunctional regulator of bone formation
    • DOI 10.2174/1381612033453659
    • Lian JB, Stein GS. Runx2/Cbfa1: a multifunctional regulator of bone formation. Curr Pharm Des 2003; 9: 2677-2685. (Pubitemid 37456017)
    • (2003) Current Pharmaceutical Design , vol.9 , Issue.32 , pp. 2677-2685
    • Lian, J.B.1    Stein, G.S.2
  • 15
    • 81255142013 scopus 로고    scopus 로고
    • Bone development: Overview of bone cells and signaling
    • Teti A. Bone development: overview of bone cells and signaling. Curr Osteoporos Rep 2011; 9: 264-273.
    • (2011) Curr Osteoporos Rep , vol.9 , pp. 264-273
    • Teti, A.1
  • 16
    • 33746061645 scopus 로고    scopus 로고
    • Inhibition of the proteasomal function in chondrocytes down-regulates growth plate chondrogenesis and longitudinal bone growth
    • DOI 10.1210/en.2005-1672
    • Wu S, De Luca F. Inhibition of the proteasomal function in chondrocytes down-regulates growth plate chondrogenesis and longitudinal bone growth. Endocrinology 2006; 147: 3761-3768. (Pubitemid 44079380)
    • (2006) Endocrinology , vol.147 , Issue.8 , pp. 3761-3768
    • Wu, S.1    De Luca, F.2
  • 17
    • 76349110797 scopus 로고    scopus 로고
    • Osteoblastogenesis and tumor growth in myeloma
    • Yaccoby S. Osteoblastogenesis and tumor growth in myeloma. Leuk Lymphoma 2010; 51: 213-220.
    • (2010) Leuk Lymphoma , vol.51 , pp. 213-220
    • Yaccoby, S.1
  • 22
    • 34548029349 scopus 로고    scopus 로고
    • Myeloma bone disease and proteasome inhibition therapies
    • DOI 10.1182/blood-2007-03-067710
    • Terpos E, Sezer O, Croucher P, Dimopoulos MA. Myeloma bone disease and proteasome inhibition therapies. Blood 2007; 110: 1098-1104. (Pubitemid 47281403)
    • (2007) Blood , vol.110 , Issue.4 , pp. 1098-1104
    • Terpos, E.1    Sezer, O.2    Croucher, P.3    Dimopoulos, M.-A.4
  • 25
    • 19644373254 scopus 로고    scopus 로고
    • Wnt signaling in disease and in development
    • DOI 10.1038/sj.cr.7290260
    • Nusse R. Wnt signaling in disease and in development. Cell Res 2005; 15: 28-32. (Pubitemid 41653961)
    • (2005) Cell Research , vol.15 , Issue.1 , pp. 28-32
    • Nusse, R.1
  • 27
    • 66149127277 scopus 로고    scopus 로고
    • Bortezomib induces osteoblast differentiation via wnt-independent activation of beta-catenin/tcf signaling
    • Qiang YW, Hu B, Chen Y, Zhong Y, Shi B, Barlogie B et al. Bortezomib induces osteoblast differentiation via Wnt-independent activation of beta-catenin/TCF signaling. Blood 2009; 113: 4319-4330.
    • (2009) Blood , vol.113 , pp. 4319-4330
    • Qiang, Y.W.1    Hu, B.2    Chen, Y.3    Zhong, Y.4    Shi, B.5    Barlogie, B.6
  • 29
    • 33746987081 scopus 로고    scopus 로고
    • The zinc finger transcription factor Gli2 mediates bone morphogenetic protein 2 expression in osteoblasts in response to hedgehog signaling
    • DOI 10.1128/MCB.02214-05
    • Zhao M, Qiao M, Harris SE, Chen D, Oyajobi BO, Mundy GR. The zinc finger transcription factor Gli2 mediates bone morphogenetic protein 2 expression in osteoblasts in response to hedgehog signaling. Mol Cell Biol 2006; 26: 6197-6208. (Pubitemid 44204537)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.16 , pp. 6197-6208
    • Zhao, M.1    Qiao, M.2    Harris, S.E.3    Chen, D.4    Oyajobi, B.O.5    Mundy, G.R.6
  • 31
    • 67649366019 scopus 로고    scopus 로고
    • Proteasome inhibitors impair rankl-induced nf-kappab activity in osteoclast-like cells via disruption of p62, traf6, cyld, and ikappabalpha signaling cascades
    • Ang E, Pavlos NJ, Rea SL, Qi M, Chai T, Walsh JP et al. Proteasome inhibitors impair RANKL-induced NF-kappaB activity in osteoclast-like cells via disruption of p62, TRAF6, CYLD, and IkappaBalpha signaling cascades. J Cell Physiol 2009; 220: 450-459.
    • (2009) J Cell Physiol , vol.220 , pp. 450-459
    • Ang, E.1    Pavlos, N.J.2    Rea, S.L.3    Qi, M.4    Chai, T.5    Walsh, J.P.6
  • 32
    • 58149478516 scopus 로고    scopus 로고
    • The proteasome inhibitor, bortezomib suppresses primary myeloma and stimulates bone formation in myelomatous and nonmyelomatous bones in vivo
    • Pennisi A, Li X, Ling W, Khan S, Zangari M, Yaccoby S. The proteasome inhibitor, bortezomib suppresses primary myeloma and stimulates bone formation in myelomatous and nonmyelomatous bones in vivo. Am J Hematol 2009; 84: 6-14.
    • (2009) Am J Hematol , vol.84 , pp. 6-14
    • Pennisi, A.1    Li, X.2    Ling, W.3    Khan, S.4    Zangari, M.5    Yaccoby, S.6
  • 33
    • 0041845297 scopus 로고    scopus 로고
    • E3 ubiquitin ligase Smurf1 mediates core-binding factor α1/Runx2 degradation and plays a specific role in osteoblast differentiation
    • DOI 10.1074/jbc.M304132200
    • Zhao M, Qiao M, Oyajobi BO, Mundy GR, Chen D. E3 ubiquitin ligase Smurf1 mediates core-binding factor alpha1/Runx2 degradation and plays a specific role in osteoblast differentiation. J Biol Chem 2003; 278: 27939-27944. (Pubitemid 36899988)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.30 , pp. 27939-27944
    • Zhao, M.1    Qiao, M.2    Oyajobi, B.O.3    Mundy, G.R.4    Chen, D.5
  • 34
    • 1842477311 scopus 로고    scopus 로고
    • Smurf1 inhibits osteoblast differentiation and bone formation in vitro and in vivo
    • DOI 10.1074/jbc.M313294200
    • Zhao M, Qiao M, Harris SE, Oyajobi BO, Mundy GR, Chen D. Smurf1 inhibits osteoblast differentiation and bone formation in vitro and in vivo. J Biol Chem 2004; 279: 12854-12859. (Pubitemid 38445859)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12854-12859
    • Zhao, M.1    Qiao, M.2    Harris, S.E.3    Oyajobi, B.O.4    Mundy, G.R.5    Chen, D.6
  • 35
    • 77952694691 scopus 로고    scopus 로고
    • Smurf1 inhibits mesenchymal stem cell proliferation and differentiation into osteoblasts through junb degradation
    • Zhao L, Huang J, Guo R, Wang Y, Chen D, Xing L. Smurf1 inhibits mesenchymal stem cell proliferation and differentiation into osteoblasts through JunB degradation. J Bone Miner Res 2010; 25: 1246-1256.
    • (2010) J Bone Miner Res , vol.25 , pp. 1246-1256
    • Zhao, L.1    Huang, J.2    Guo, R.3    Wang, Y.4    Chen, D.5    Xing, L.6
  • 36
  • 37
    • 53149122891 scopus 로고    scopus 로고
    • Ubiquitin ligase smurf1 mediates tumor necrosis factor-induced systemic bone loss by promoting proteasomal degradation of bone morphogenetic signaling proteins
    • Guo R, Yamashita M, Zhang Q, Zhou Q, Chen D, Reynolds DG et al. Ubiquitin ligase Smurf1 mediates tumor necrosis factor-induced systemic bone loss by promoting proteasomal degradation of bone morphogenetic signaling proteins. J Biol Chem 2008; 283: 23084-23092.
    • (2008) J Biol Chem , vol.283 , pp. 23084-23092
    • Guo, R.1    Yamashita, M.2    Zhang, Q.3    Zhou, Q.4    Chen, D.5    Reynolds, D.G.6
  • 38
    • 37248998857 scopus 로고    scopus 로고
    • Control of postnatal bone mass by the zinc finger adapter protein Schnurri-3
    • DOI 10.1196/annals.1402.044, Skeletal Biology and Medicine, Part A: Aspects of Bone Morphogenesis and Remodeling
    • Glimcher LH, Jones DC, Wein MN. Control of postnatal bone mass by the zinc finger adapter protein Schnurri-3. Ann N Y Acad Sci 2007; 1116: 174-181. (Pubitemid 350274333)
    • (2007) Annals of the New York Academy of Sciences , vol.1116 , pp. 174-181
    • Glimcher, L.H.1    Jones, D.C.2    Wein, M.N.3
  • 40
    • 0033549789 scopus 로고    scopus 로고
    • A smad ubiquitin ligase targets the bmp pathway and affects embryonic pattern formation
    • Zhu H, Kavsak P, Abdollah S, Wrana JL, Thomsen GH. A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation. Nature 1999; 400: 687-693.
    • (1999) Nature , vol.400 , pp. 687-693
    • Zhu, H.1    Kavsak, P.2    Abdollah, S.3    Wrana, J.L.4    Thomsen, G.H.5
  • 41
    • 84862777472 scopus 로고    scopus 로고
    • A delivery system targeting bone formation surfaces to facilitate rnai-based anabolic therapy
    • Zhang G, Guo B, Wu H, Tang T, Zhang BT, Zheng L et al. A delivery system targeting bone formation surfaces to facilitate RNAi-based anabolic therapy. Nat Med 2012; 18: 307-314.
    • (2012) Nat Med , vol.18 , pp. 307-314
    • Zhang, G.1    Guo, B.2    Wu, H.3    Tang, T.4    Zhang, B.T.5    Zheng, L.6
  • 42
    • 10744231292 scopus 로고    scopus 로고
    • Proteasomal degradation of Runx2 shortens parathyroid hormone-induced anti-apoptotic signaling in osteoblasts: A putative explanation for why intermittent administration is needed for bone anabolism
    • DOI 10.1074/jbc.M307444200
    • Bellido T, Ali AA, Plotkin LI, Fu Q, Gubrij I, Roberson PK et al. Proteasomal degradation of Runx2 shortens parathyroid hormone-induced anti-Apoptotic signaling in osteoblasts. A putative explanation for why intermittent administration is needed for bone anabolism. J Biol Chem 2003; 278: 50259-50272. (Pubitemid 37548867)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 50259-50272
    • Bellido, T.1    Ali, A.A.2    Plotkin, L.I.3    Fu, Q.4    Gubrij, I.5    Roberson, P.K.6    Weinstein, R.S.7    O'Brien, C.A.8    Manolagas, S.C.9    Jilka, R.L.10
  • 43
    • 17044414102 scopus 로고    scopus 로고
    • Ubiquitin ligase smurf1 controls osteoblast activity and bone homeostasis by targeting mekk2 for degradation
    • Yamashita M, Ying SX, Zhang GM, Li C, Cheng SY, Deng CX et al. Ubiquitin ligase Smurf1 controls osteoblast activity and bone homeostasis by targeting MEKK2 for degradation. Cell 2005; 121: 101-113.
    • (2005) Cell , vol.121 , pp. 101-113
    • Yamashita, M.1    Ying, S.X.2    Zhang, G.M.3    Li, C.4    Cheng, S.Y.5    Deng, C.X.6
  • 45
    • 33744454653 scopus 로고    scopus 로고
    • Regulation of adult bone mass by the zinc finger adapter protein Schnurri-3
    • DOI 10.1126/science.1126313
    • Jones DC, Wein MN, Oukka M, Hofstaetter JG, Glimcher MJ, Glimcher LH. Regulation of adult bone mass by the zinc finger adapter protein Schnurri-3. Science 2006; 312: 1223-1227. (Pubitemid 43801150)
    • (2006) Science , vol.312 , Issue.5777 , pp. 1223-1227
    • Jones, D.C.1    Wein, M.N.2    Oukka, M.3    Hofstaetter, J.G.4    Glimcher, M.J.5    Glimcher, L.H.6
  • 46
    • 80053281947 scopus 로고    scopus 로고
    • Tumor necrosis factor inhibits mesenchymal stem cell differentiation into osteoblasts via the ubiquitin e3 ligase wwp1
    • Zhao L, Huang J, Zhang H, Wang Y, Matesic LE, Takahata M et al. Tumor necrosis factor inhibits mesenchymal stem cell differentiation into osteoblasts via the ubiquitin E3 ligase Wwp1. Stem Cells 2011; 29: 1601-1610.
    • (2011) Stem Cells , vol.29 , pp. 1601-1610
    • Zhao, L.1    Huang, J.2    Zhang, H.3    Wang, Y.4    Matesic, L.E.5    Takahata, M.6
  • 47
    • 8744224520 scopus 로고    scopus 로고
    • ATF4, the osteoblast accumulation of which is determined post-translationally, can induce osteoblast-specific gene expression in non-osteoblastic cells
    • DOI 10.1074/jbc.M410010200
    • Yang X, Karsenty G. ATF4, the osteoblast accumulation of which is determined post-translationally, can induce osteoblast-specific gene expression in non-osteoblastic cells. J Biol Chem 2004; 279: 47109-47114. (Pubitemid 39518367)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.45 , pp. 47109-47114
    • Yang, X.1    Karsenty, G.2
  • 48
    • 51049115529 scopus 로고    scopus 로고
    • A new ubiquitin ligase involved in p57kip2 proteolysis regulates osteoblast cell differentiation
    • Kim M, Nakamoto T, Nishimori S, Tanaka K, Chiba T. A new ubiquitin ligase involved in p57KIP2 proteolysis regulates osteoblast cell differentiation. EMBO Rep 2008; 9: 878-884.
    • (2008) EMBO Rep , vol.9 , pp. 878-884
    • Kim, M.1    Nakamoto, T.2    Nishimori, S.3    Tanaka, K.4    Chiba, T.5
  • 49
    • 0141637441 scopus 로고    scopus 로고
    • Cbl signaling networks in the regulation of cell function
    • DOI 10.1007/s00018-003-3029-4
    • Dikic I, Szymkiewicz I, Soubeyran P. Cbl signaling networks in the regulation of cell function. Cell Mol Life Sci 2003; 60: 1805-1827. (Pubitemid 37222580)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.9 , pp. 1805-1827
    • Dikic, I.1    Szymkiewicz, I.2    Soubeyran, P.3
  • 50
    • 33748196233 scopus 로고    scopus 로고
    • The Cbl family proteins: Ring leaders in regulation of cell signaling
    • DOI 10.1002/jcp.20694
    • Swaminathan G, Tsygankov AY. The Cbl family proteins: ring leaders in regulation of cell signaling. J Cell Physiol 2006; 209: 21-43. (Pubitemid 44318665)
    • (2006) Journal of Cellular Physiology , vol.209 , Issue.1 , pp. 21-43
    • Swaminathan, G.1    Tsygankov, A.Y.2
  • 51
    • 84869112362 scopus 로고    scopus 로고
    • Protein tyrosine kinase regulation by ubiquitination: Critical roles of cbl-family ubiquitin ligases
    • Mohapatra B, Ahmad G, Nadeau S, Zutshi N, An W, Scheffe S et al. Protein tyrosine kinase regulation by ubiquitination: Critical roles of Cbl-family ubiquitin ligases. Biochim Biophys Acta 2013; 1833: 122-139.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 122-139
    • Mohapatra, B.1    Ahmad, G.2    Nadeau, S.3    Zutshi, N.4    An, W.5    Scheffe, S.6
  • 52
    • 0035316576 scopus 로고    scopus 로고
    • Cbl: Many adaptations to regulate protein tyrosine kinases
    • Thien CB, Langdon WY. Cbl: many adaptations to regulate protein tyrosine kinases. Nat Rev Mol Cell Biol 2001; 2: 294-307.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 294-307
    • Thien, C.B.1    Langdon, W.Y.2
  • 53
    • 0035473477 scopus 로고    scopus 로고
    • Beyond the RING: CBL proteins as multivalent adapters
    • DOI 10.1038/sj.onc.1204781
    • Tsygankov AY, Teckchandani AM, Feshchenko EA, Swaminathan G. Beyond the RING: CBL proteins as multivalent adapters. Oncogene 2001; 20: 6382-6402. (Pubitemid 32977846)
    • (2001) Oncogene , vol.20 , Issue.44 REV. ISS. 5 , pp. 6382-6402
    • Tsygankov, A.Y.1    Teckchandani, A.M.2    Feshchenko, E.A.3    Swaminathan, G.4
  • 54
    • 28844490931 scopus 로고    scopus 로고
    • The cbl interactome and its functions
    • Schmidt MH, Dikic I. The Cbl interactome and its functions. Nat Rev Mol Cell Biol 2005; 6: 907-919.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 907-919
    • Schmidt, M.H.1    Dikic, I.2
  • 55
    • 23744489852 scopus 로고    scopus 로고
    • Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation
    • DOI 10.1038/sj.embor.7400453
    • Haglund K, Schmidt MH, Wong ES, Guy GR, Dikic I. Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation. EMBO Rep 2005; 6: 635-641. (Pubitemid 41122431)
    • (2005) EMBO Reports , vol.6 , Issue.7 , pp. 635-641
    • Haglund, K.1    Schmidt, M.H.H.2    Wong, E.S.M.3    Guy, G.R.4    Dikic, I.5
  • 56
    • 3142618052 scopus 로고    scopus 로고
    • Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations
    • DOI 10.1074/jbc.M404114200
    • Kassenbrock CK, Anderson SM. Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations. J Biol Chem 2004; 279: 28017-28027. (Pubitemid 38900072)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 28017-28027
    • Kassenbrock, C.K.1    Anderson, S.M.2
  • 57
  • 59
    • 24944538477 scopus 로고    scopus 로고
    • Negative regulation of PTK signalling by Cbl proteins
    • DOI 10.1080/08977190500153763, PII U440137727600
    • Thien CB, Langdon WY. Negative regulation of PTK signalling by Cbl proteins. Growth Factors 2005; 23: 161-167. (Pubitemid 43203064)
    • (2005) Growth Factors , vol.23 , Issue.2 , pp. 161-167
    • Thien, C.B.F.1    Langdon, W.Y.2
  • 60
    • 0033593322 scopus 로고    scopus 로고
    • Fyn associates with cbl and phosphorylates tyrosine 731 in cbl, a binding site for phosphatidylinositol 3-kinase
    • Hunter S, Burton EA, Wu SC, Anderson SM. Fyn associates with Cbl and phosphorylates tyrosine 731 in Cbl, a binding site for phosphatidylinositol 3-kinase. J Biol Chem 1999; 274: 2097-2106.
    • (1999) J Biol Chem , vol.274 , pp. 2097-2106
    • Hunter, S.1    Burton, E.A.2    Wu, S.C.3    Anderson, S.M.4
  • 61
    • 4844227729 scopus 로고    scopus 로고
    • Cbl-b interacts with ubiquitinated proteins; differential functions of the UBA domains of c-Cbl and Cbl-b
    • DOI 10.1038/sj.onc.1207952
    • Davies GC, Ettenberg SA, Coats AO, Mussante M, Ravichandran S, Collins J et al. Cbl-b interacts with ubiquitinated proteins; differential functions of the UBA domains of c-Cbl and Cbl-b. Oncogene 2004; 23: 7104-7115. (Pubitemid 39319172)
    • (2004) Oncogene , vol.23 , Issue.42 , pp. 7104-7115
    • Bavies, G.C.1    Ettenberg, S.A.2    Coats, A.O.3    Mussante, M.4    Ravichandran, S.5    Collins, J.6    Nau, M.M.7    Lipkowitz, S.8
  • 63
    • 0037376901 scopus 로고    scopus 로고
    • Negative receptor signalling
    • DOI 10.1016/S0955-0674(03)00004-8
    • Dikic I, Giordano S. Negative receptor signalling. Curr Opin Cell Biol 2003; 15: 128-135. (Pubitemid 36332186)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.2 , pp. 128-135
    • Dikic, I.1    Giordano, S.2
  • 64
    • 19644367829 scopus 로고    scopus 로고
    • Negative regulation of receptor tyrosine kinases: Unexpected links to c-Cbl and receptor ubiquitylation
    • DOI 10.1038/sj.cr.7290268
    • Rubin C, Gur G, Yarden Y. Negative regulation of receptor tyrosine kinases: unexpected links to c-Cbl and receptor ubiquitylation. Cell Res 2005; 15: 66-71. (Pubitemid 41653969)
    • (2005) Cell Research , vol.15 , Issue.1 , pp. 66-71
    • Rubin, C.1    Gur, G.2    Yarden, Y.3
  • 65
    • 0036911112 scopus 로고    scopus 로고
    • C-Cbl and Cbl-b regulate T cell responsiveness by promoting ligand-induced TCR down-modulation
    • DOI 10.1038/ni855
    • Naramura M, Jang IK, Kole H, Huang F, Haines D, Gu H. c-Cbl and Cbl-b regulate T cell responsiveness by promoting ligand-induced TCR down-modulation. Nat Immunol 2002; 3: 1192-1199. (Pubitemid 35469704)
    • (2002) Nature Immunology , vol.3 , Issue.12 , pp. 1192-1199
    • Naramura, M.1    Jang, I.-K.2    Kole, H.3    Huang, F.4    Haines, D.5    Gu, H.6
  • 66
    • 0042386646 scopus 로고    scopus 로고
    • Deletion of the gene encoding c-Cbl alters the ability of osteoclasts to migrate, delaying resorption and ossification of cartilage during the development of long bones
    • DOI 10.1016/S0012-1606(03)00299-9
    • Chiusaroli R, Sanjay A, Henriksen K, Engsig MT, Horne WC, Gu H et al. Deletion of the gene encoding c-Cbl alters the ability of osteoclasts to migrate, delaying resorption and ossification of cartilage during the development of long bones. Dev Biol 2003; 261: 537-547. (Pubitemid 37108791)
    • (2003) Developmental Biology , vol.261 , Issue.2 , pp. 537-547
    • Chiusaroli, R.1    Sanjay, A.2    Henriksen, K.3    Engsig, M.T.4    Horne, W.C.5    Gu, H.6    Baron, R.7
  • 67
    • 21844437618 scopus 로고    scopus 로고
    • Dynamin forms a Src kinase-sensitive complex with Cbl and regulates podosomes and osteoclast activity
    • DOI 10.1091/mbc.E04-12-1117
    • Bruzzaniti A, Neff L, Sanjay A, Horne WC, De Camilli P, Baron R. Dynamin forms a Src kinase-sensitive complex with Cbl and regulates podosomes and osteoclast activity. Mol Biol Cell 2005; 16: 3301-3313. (Pubitemid 40962599)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.7 , pp. 3301-3313
    • Bruzzaniti, A.1    Neff, L.2    Sanjay, A.3    Horne, W.C.4    De Camilli, P.5    Baron, R.6
  • 68
    • 0032479979 scopus 로고    scopus 로고
    • 1 integrin signaling pathway involving Src-family kinases, Cbl and PI-3 kinase is required for macrophage spreading and migration
    • DOI 10.1093/emboj/17.15.4391
    • Meng F, Lowell CA. A beta 1 integrin signaling pathway involving Src-family kinases, Cbl and PI-3 kinase is required for macrophage spreading and migration. EMBO J 1998; 17: 4391-4403. (Pubitemid 28362629)
    • (1998) EMBO Journal , vol.17 , Issue.15 , pp. 4391-4403
    • Meng, F.1    Lowell, C.A.2
  • 70
    • 28544451132 scopus 로고    scopus 로고
    • The role(s) of Src kinase and Cbl proteins in the regulation of osteoclast differentiation and function
    • Horne WC, Sanjay A, Bruzzaniti A, Baron R. The role(s) of Src kinase and Cbl proteins in the regulation of osteoclast differentiation and function. Immunol Rev 2005; 208: 106-125. (Pubitemid 41746388)
    • (2005) Immunological Reviews , vol.208 , pp. 106-125
    • Horne, W.C.1    Sanjay, A.2    Bruzzaniti, A.3    Baron, R.4
  • 71
    • 70350230150 scopus 로고    scopus 로고
    • C-cbl and cbl-b act redundantly to protect osteoclasts from apoptosis and to displace hdac6 from beta-tubulin, stabilizing microtubules and podosomes
    • Purev E, Neff L, Horne WC, Baron R. c-Cbl and Cbl-b act redundantly to protect osteoclasts from apoptosis and to displace HDAC6 from beta-tubulin, stabilizing microtubules and podosomes. Mol Biol Cell 2009; 20: 4021-4030.
    • (2009) Mol Biol Cell , vol.20 , pp. 4021-4030
    • Purev, E.1    Neff, L.2    Horne, W.C.3    Baron, R.4
  • 72
    • 0029858150 scopus 로고    scopus 로고
    • C-Cbl is downstream of c-Src in a signalling pathway necessary for bone resorption
    • DOI 10.1038/383528a0
    • Tanaka S, Amling M, Neff L, Peyman A, Uhlmann E, Levy JB et al. c-Cbl is downstream of c-Src in a signalling pathway necessary for bone resorption. Nature 1996; 383: 528-531. (Pubitemid 26346179)
    • (1996) Nature , vol.383 , Issue.6600 , pp. 528-531
    • Tanaka, S.1    Amling, M.2    Neff, L.3    Peyman, A.4    Uhlmann, E.5    Levy, J.B.6    Baron, R.7
  • 73
    • 0035860713 scopus 로고    scopus 로고
    • Src-catalyzed phosphorylation of c-cbl leads to the interdependent ubiquitination of both proteins
    • Yokouchi M, Kondo T, Sanjay A, Houghton A, Yoshimura A, Komiya S et al. Src-catalyzed phosphorylation of c-Cbl leads to the interdependent ubiquitination of both proteins. J Biol Chem 2001; 276: 35185-35193.
    • (2001) J Biol Chem , vol.276 , pp. 35185-35193
    • Yokouchi, M.1    Kondo, T.2    Sanjay, A.3    Houghton, A.4    Yoshimura, A.5    Komiya, S.6
  • 75
    • 78449236806 scopus 로고    scopus 로고
    • The loss of cbl-phosphatidylinositol 3-kinase interaction perturbs rankl-mediated signaling, inhibiting bone resorption and promoting osteoclast survival
    • Adapala NS, Barbe MF, Langdon WY, Nakamura MC, Tsygankov AY, Sanjay A. The loss of Cbl-phosphatidylinositol 3-kinase interaction perturbs RANKL-mediated signaling, inhibiting bone resorption and promoting osteoclast survival. J Biol Chem 2010; 285: 36745-36758.
    • (2010) J Biol Chem , vol.285 , pp. 36745-36758
    • Adapala, N.S.1    Barbe, M.F.2    Langdon, W.Y.3    Nakamura, M.C.4    Tsygankov, A.Y.5    Sanjay, A.6
  • 76
    • 79959908795 scopus 로고    scopus 로고
    • The casitas b lineage lymphoma (cbl) mutant g306e enhances osteogenic differentiation in human mesenchymal stromal cells in part by decreased cbl-mediated platelet-derived growth factor receptor alpha and fibroblast growth factor receptor 2 ubiquitination
    • Sévére N, Miraoui H, Marie PJ. The Casitas B lineage lymphoma (Cbl) mutant G306E enhances osteogenic differentiation in human mesenchymal stromal cells in part by decreased Cbl-mediated platelet-derived growth factor receptor alpha and fibroblast growth factor receptor 2 ubiquitination. J Biol Chem 2011; 286: 24443-24450.
    • (2011) J Biol Chem , vol.286 , pp. 24443-24450
    • Sévére, N.1    Miraoui, H.2    Marie, P.J.3
  • 77
    • 0942300656 scopus 로고    scopus 로고
    • The expanding role of PI3-kinase in bone
    • DOI 10.1016/j.bone.2003.09.005
    • Golden LH, Insogna KL. The expanding role of PI3-kinase in bone. Bone 2004; 34: 3-12. (Pubitemid 38142429)
    • (2004) Bone , vol.34 , Issue.1 , pp. 3-12
    • Golden, L.H.1    Insogna, K.L.2
  • 78
    • 82755182581 scopus 로고    scopus 로고
    • Abrogation of cbl-pi3k interaction increases bone formation and osteoblast proliferation
    • Brennan T, Adapala NS, Barbe MF, Yingling V, Sanjay A. Abrogation of Cbl-PI3K interaction increases bone formation and osteoblast proliferation. Calcif Tissue Int 2011; 89: 396-410.
    • (2011) Calcif Tissue Int , vol.89 , pp. 396-410
    • Brennan, T.1    Adapala, N.S.2    Barbe, M.F.3    Yingling, V.4    Sanjay, A.5
  • 79
    • 0035016726 scopus 로고    scopus 로고
    • Increased bone formation and decreased osteocalcin expression induced by reduced twist dosage in Saethre-Chotzen syndrome
    • Yousfi M, Lasmoles F, Lomri A, Delannoy P, Marie PJ. Increased bone formation and decreased osteocalcin expression induced by reduced Twist dosage in Saethre-Chotzen syndrome. J Clin Invest 2001; 107: 1153-1161. (Pubitemid 32422912)
    • (2001) Journal of Clinical Investigation , vol.107 , Issue.9 , pp. 1153-1161
    • Yousfi, M.1    Lasmoles, F.2    Lomri, A.3    Delannoy, P.4    Marie, P.J.5
  • 80
    • 38849132555 scopus 로고    scopus 로고
    • Down-regulation of ubiquitin ligase Cbl induced by twist haploinsufficiency in Saethre-Chotzen syndrome results in increased PI3K/Akt signaling and osteoblast proliferation
    • DOI 10.2353/ajpath.2006.060102
    • Guénou H, Kaabeche K, Dufour C, Miraoui H, Marie PJ. Down-regulation of ubiquitin ligase Cbl induced by twist haploinsufficiency in Saethre-Chotzen syndrome results in increased PI3K/Akt signaling and osteoblast proliferation. Am J Pathol 2006; 169: 1303-1311. (Pubitemid 351194365)
    • (2006) American Journal of Pathology , vol.169 , Issue.4 , pp. 1303-1311
    • Guenou, H.1    Kaabeche, K.2    Dufour, C.3    Miraoui, H.4    Marie, P.J.5
  • 81
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon MA, Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 2010; 141: 1117-1134.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 82
    • 0033536637 scopus 로고    scopus 로고
    • The tyrosine kinase negative regulator c-Cbl as a RING-type, E2- dependent ubiquitin-protein ligase
    • DOI 10.1126/science.286.5438.309
    • Joazeiro CA, Wing SS, Huang H, Leverson JD, Hunter T, Liu YC. The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase. Science 1999; 286: 309-312. (Pubitemid 29484697)
    • (1999) Science , vol.286 , Issue.5438 , pp. 309-312
    • Joazeiro, C.A.P.1    Wing, S.S.2    Huang, H.-K.3    Leverson, J.D.4    Hunter, T.5    Liu, Y.-C.6
  • 84
    • 0033523010 scopus 로고    scopus 로고
    • Cbl-mediated negative regulation of platelet-derived growth factor receptor-dependent cell proliferation. A critical role for cbl tyrosine kinase-binding domain
    • Miyake S, Mullane-Robinson KP, Lill NL, Douillard P, Band H. Cbl-mediated negative regulation of platelet-derived growth factor receptor-dependent cell proliferation. A critical role for Cbl tyrosine kinase-binding domain. J Biol Chem 1999; 274: 16619-16628.
    • (1999) J Biol Chem , vol.274 , pp. 16619-16628
    • Miyake, S.1    Mullane-Robinson, K.P.2    Lill, N.L.3    Douillard, P.4    Band, H.5
  • 85
    • 0033615732 scopus 로고    scopus 로고
    • Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-cbl ring finger and ubch7
    • Yokouchi M, Kondo T, Houghton A, Bartkiewicz M, Horne WC, Zhang H et al. Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7. J Biol Chem 1999; 274: 31707-31712.
    • (1999) J Biol Chem , vol.274 , pp. 31707-31712
    • Yokouchi, M.1    Kondo, T.2    Houghton, A.3    Bartkiewicz, M.4    Horne, W.C.5    Zhang, H.6
  • 86
    • 42349108970 scopus 로고    scopus 로고
    • A tale of two Cbls: Interplay of c-Cbl and Cbl-b in epidermal growth factor receptor downregulation
    • DOI 10.1128/MCB.01809-07
    • Pennock S, Wang Z. A tale of two Cbls: interplay of c-Cbl and Cbl-b in epidermal growth factor receptor downregulation. Mol Cell Biol 2008; 28: 3020-3037. (Pubitemid 351556533)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.9 , pp. 3020-3037
    • Pennock, S.1    Wang, Z.2
  • 87
    • 84865787955 scopus 로고    scopus 로고
    • The insulin-like growth factor system in bone: Basic and clinical implications. Endocrinol metab clin north am 2012; 41: 323-333; vi. 88. Mohan s, kesavan c. Role of insulin-like growth factor-1 in the regulation of skeletal growth
    • Kawai M, Rosen CJ. The insulin-like growth factor system in bone: basic and clinical implications. Endocrinol Metab Clin North Am 2012; 41: 323-333; vi. 88. Mohan S, Kesavan C. Role of insulin-like growth factor-1 in the regulation of skeletal growth. Curr Osteoporos Rep 2012; 10: 178-186.
    • (2012) Curr Osteoporos Rep , vol.10 , pp. 178-186
    • Kawai, M.1    Rosen, C.J.2
  • 88
    • 84858960891 scopus 로고    scopus 로고
    • Fgf/fgfr signaling in bone formation: Progress and perspectives
    • Marie PJ, Miraoui H, Sévére N. FGF/FGFR signaling in bone formation: progress and perspectives. Growth Factors 2012; 30: 117-123.
    • (2012) Growth Factors , vol.30 , pp. 117-123
    • Marie, P.J.1    Miraoui, H.2    Sévére, N.3
  • 89
    • 84865441732 scopus 로고    scopus 로고
    • Role of fgfs/fgfrs in skeletal development and bone regeneration
    • Du X, Xie Y, Xian CJ, Chen L. Role of FGFs/FGFRs in skeletal development and bone regeneration. J Cell Physiol 2012; 227: 3731-3743.
    • (2012) J Cell Physiol , vol.227 , pp. 3731-3743
    • Du, X.1    Xie, Y.2    Xian, C.J.3    Chen, L.4
  • 90
    • 84858159772 scopus 로고    scopus 로고
    • Fibroblast growth factor signaling controlling bone formation: An update
    • Marie PJ. Fibroblast growth factor signaling controlling bone formation: an update. Gene 2012; 498: 1-4.
    • (2012) Gene , vol.498 , pp. 1-4
    • Marie, P.J.1
  • 91
    • 20344363684 scopus 로고    scopus 로고
    • Cell Signalling: Mechanism of divergent growth factor effects in mesenchymal stem cell differentiation
    • DOI 10.1126/science.1107627
    • Kratchmarova I, Blagoev B, Haack-Sorensen M, Kassem M, Mann M. Mechanism of divergent growth factor effects in mesenchymal stem cell differentiation. Science 2005; 308: 1472-1477. (Pubitemid 40791302)
    • (2005) Science , vol.308 , Issue.5727 , pp. 1472-1477
    • Kratchmarova, I.1    Blagoev, B.2    Haack-Sorensen, M.3    Kassem, M.4    Mann, M.5
  • 92
    • 0037097976 scopus 로고    scopus 로고
    • FGF signaling pathways in endochondral and intramembranous bone development and human genetic disease
    • DOI 10.1101/gad.990702
    • Ornitz DM, Marie PJ. FGF signaling pathways in endochondral and intramembranous bone development and human genetic disease. Genes Dev 2002; 16: 1446-1465. (Pubitemid 34686327)
    • (2002) Genes and Development , vol.16 , Issue.12 , pp. 1446-1465
    • Ornitz, D.M.1    Marie, P.J.2
  • 94
    • 0035058533 scopus 로고    scopus 로고
    • Role of N-cadherin and protein kinase C in osteoblast gene activation induced by the S252W fibroblast growth factor receptor 2 mutation in apert craniosynostosis
    • Lemonnier J, Hay̌ E, Delannoy P, Lomri A, Modrowski D, Caverzasio J et al. Role of N-cadherin and protein kinase C in osteoblast gene activation induced by the S252W fibroblast growth factor receptor 2 mutation in Apert craniosynostosis. J Bone Miner Res 2001; 16: 832-845. (Pubitemid 32332293)
    • (2001) Journal of Bone and Mineral Research , vol.16 , Issue.5 , pp. 832-845
    • Lemonnier, J.1    Hay, E.2    Delannoy, P.3    Lomri, A.4    Modrowski, D.5    Caverzasio, J.6    Marie, P.J.7
  • 95
    • 0035081456 scopus 로고    scopus 로고
    • Increased expression of protein kinase Cα, interleukin-1 α, and RhoA guanosine 5′-triphosphatase in osteoblasts expressing the Ser252Trp fibroblast growth factor 2 Apert mutation: Identification by analysis of complementary DNA microarray
    • Lomri A, Lemonnier J, Delannoy P, Marie PJ. Increased expression of protein kinase Calpha, interleukin-1alpha, and RhoA guanosine 50-triphosphatase in osteoblasts expressing the Ser252Trp fibroblast growth factor 2 receptor Apert mutation: identification by analysis of complementary DNA microarray. J Bone Miner Res 2001; 16: 705-712. (Pubitemid 32230599)
    • (2001) Journal of Bone and Mineral Research , vol.16 , Issue.4 , pp. 705-712
    • Lomri, A.1    Lemonnier, J.2    Delannoy, P.3    Marie, P.J.4
  • 96
    • 64149095856 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor 2 promotes osteogenic differentiation in mesenchymal cells via erk1/2 and protein kinase c signaling
    • Miraoui H, Oudina K, Petite H, Tanimoto Y, Moriyama K, Marie PJ. Fibroblast growth factor receptor 2 promotes osteogenic differentiation in mesenchymal cells via ERK1/2 and protein kinase C signaling. J Biol Chem 2009; 284: 4897-4904.
    • (2009) J Biol Chem , vol.284 , pp. 4897-4904
    • Miraoui, H.1    Oudina, K.2    Petite, H.3    Tanimoto, Y.4    Moriyama, K.5    Marie, P.J.6
  • 97
    • 77952529135 scopus 로고    scopus 로고
    • Increased efg and pdgf{alpha}-receptor signaling by mutant fgf-receptor 2 contributes to osteoblast dysfunction in apert craniosynostosis
    • Miraoui H, Ringe J, Haupl T, Marie PJ. Increased EFG- And PDGF{alpha}-receptor signaling by mutant FGF-receptor 2 contributes to osteoblast dysfunction in Apert craniosynostosis. Hum Mol Genet 2010; 19: 1678-1689.
    • (2010) Hum Mol Genet , vol.19 , pp. 1678-1689
    • Miraoui, H.1    Ringe, J.2    Haupl, T.3    Marie, P.J.4
  • 98
    • 78049497367 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor signaling crosstalk in skeletogenesis
    • Miraoui H, Marie PJ. Fibroblast growth factor receptor signaling crosstalk in skeletogenesis. Sci Signal 2010; 3: re9.
    • (2010) Sci Signal , vol.3
    • Miraoui, H.1    Marie, P.J.2
  • 100
    • 4344624316 scopus 로고    scopus 로고
    • Cbl-mediated degradation of Lyn and Fyn induced by constitutive fibroblast growth factor receptor-2 activation supports osteoblast differentiation
    • DOI 10.1074/jbc.M402469200
    • Kaabeche K, Lemonnier J, Le Mée S, Caverzasio J, Marie PJ. Cbl-mediated degradation of Lyn and Fyn induced by constitutive fibroblast growth factor receptor-2 activation supports osteoblast differentiation. J Biol Chem 2004; 279: 36259-36267. (Pubitemid 39128962)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.35 , pp. 36259-36267
    • Kaabeche, K.1    Lemonnier, J.2    Le Mee, S.3    Caverzasio, J.4    Marie, P.J.5
  • 101
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • DOI 10.1093/emboj/17.24.7151
    • Ciechanover A. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J 1998; 17: 7151-7160. (Pubitemid 29002684)
    • (1998) EMBO Journal , vol.17 , Issue.24 , pp. 7151-7160
    • Ciechanover, A.1
  • 102
    • 23944507555 scopus 로고    scopus 로고
    • Discovery of the ubiquitin proteasome system and its involvement in apoptosis
    • DOI 10.1038/sj.cdd.4401740
    • Melino G. Discovery of the ubiquitin proteasome system and its involvement in apoptosis. Cell Death Differ 2005; 12: 1155-1157. (Pubitemid 41195098)
    • (2005) Cell Death and Differentiation , vol.12 , Issue.9 , pp. 1155-1157
    • Melino, G.1
  • 103
    • 17244380370 scopus 로고    scopus 로고
    • Cbl-mediated ubiquitination of α5 integrin subunit mediates fibronectin-dependent osteoblast detachment and apoptosis induced by FGFR2 activation
    • DOI 10.1242/jcs.01679
    • Kaabeche K, Guénou H, Bouvard D, Didelot N, Listrat A, Marie PJ. Cbl-mediated ubiquitination of alpha5 integrin subunit mediates fibronectin-dependent osteoblast detachment and apoptosis induced by FGFR2 activation. J Cell Sci 2005; 118(Pt 6): 1223-1232. (Pubitemid 40528692)
    • (2005) Journal of Cell Science , vol.118 , Issue.6 , pp. 1223-1232
    • Kaabeche, K.1    Guenou, H.2    Bouvard, D.3    Didelot, N.4    Listrat, A.5    Marie, P.J.6
  • 104
    • 0037193470 scopus 로고    scopus 로고
    • Cosignaling of NCAM via lipid rafts and the FGF receptor is required for neuritogenesis
    • DOI 10.1083/jcb.200109059
    • Niethammer P, Delling M, Sytnyk V, Dityatev A, Fukami K, Schachner M. Cosignaling of NCAM via lipid rafts and the FGF receptor is required for neuritogenesis. J Cell Biol 2002; 157: 521-532. (Pubitemid 34839814)
    • (2002) Journal of Cell Biology , vol.157 , Issue.3 , pp. 521-532
    • Niethammer, P.1    Delling, M.2    Sytnyk, V.3    Dityatev, A.4    Fukami, K.5    Schachner, M.6
  • 105
    • 3042730952 scopus 로고    scopus 로고
    • Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites
    • DOI 10.1242/jcs.01148
    • Haglund K, Ivankovic-Dikic I, Shimokawa N, Kruh GD, Dikic I. Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites. J Cell Sci 2004; 117(Pt 12): 2557-2568. (Pubitemid 38877851)
    • (2004) Journal of Cell Science , vol.117 , Issue.12 , pp. 2557-2568
    • Haglund, K.1    Ivankovic-Dikic, I.2    Shimokawa, N.3    Kruh, G.D.4    Dikic, I.5
  • 107
    • 43149123990 scopus 로고    scopus 로고
    • Fgfr2-cbl interaction in lipid rafts triggers attenuation of pi3k/akt signaling and osteoblast survival
    • Dufour C, Guénou H, Kaabeche K, Bouvard D, Sanjay A, Marie PJ. FGFR2-Cbl interaction in lipid rafts triggers attenuation of PI3K/Akt signaling and osteoblast survival. Bone 2008; 42: 1032-1039.
    • (2008) Bone , vol.42 , pp. 1032-1039
    • Dufour, C.1    Guénou, H.2    Kaabeche, K.3    Bouvard, D.4    Sanjay, A.5    Marie, P.J.6
  • 108
    • 77954582429 scopus 로고    scopus 로고
    • Cbl-b enhances runx2 protein stability and augments osteocalcin promoter activity in osteoblastic cell lines
    • Salingcarnboriboon RA, Pavasant P, Noda M. Cbl-b enhances Runx2 protein stability and augments osteocalcin promoter activity in osteoblastic cell lines. J Cell Physiol 2010; 224: 743-747.
    • (2010) J Cell Physiol , vol.224 , pp. 743-747
    • Salingcarnboriboon, R.A.1    Pavasant, P.2    Noda, M.3
  • 109
    • 33646227897 scopus 로고    scopus 로고
    • Ubiquitin ligase cblb downregulates bone formation through suppression of igf-i signaling in osteoblasts during denervation
    • Suzue N, Nikawa T, Onishi Y, Yamada C, Hirasaka K, Ogawa T et al. Ubiquitin ligase Cblb downregulates bone formation through suppression of IGF-I signaling in osteoblasts during denervation. J Bone Miner Res 2006; 21: 722-734.
    • (2006) J Bone Miner Res , vol.21 , pp. 722-734
    • Suzue, N.1    Nikawa, T.2    Onishi, Y.3    Yamada, C.4    Hirasaka, K.5    Ogawa, T.6
  • 110
    • 79952453470 scopus 로고    scopus 로고
    • High-throughput fluorescence polarization assay to identify inhibitors of cbl(tkb)-protein tyrosine kinase interactions
    • Kumar EA, Charvet CD, Lokesh GL, Natarajan A. High-throughput fluorescence polarization assay to identify inhibitors of Cbl(TKB)-protein tyrosine kinase interactions. Anal Biochem 2011; 411: 254-260.
    • (2011) Anal Biochem , vol.411 , pp. 254-260
    • Kumar, E.A.1    Charvet, C.D.2    Lokesh, G.L.3    Natarajan, A.4
  • 111
    • 9644272423 scopus 로고    scopus 로고
    • The ubiquitin system: Pathogenesis of human diseases and drug targeting
    • DOI 10.1016/j.bbamcr.2004.09.018, PII S0167488904002344, The Ubiquitin-Proteasome System
    • Ciechanover A, Schwartz AL. The ubiquitin system: pathogenesis of human diseases and drug targeting. Biochim Biophys Acta 2004; 1695: 3-17. (Pubitemid 39574964)
    • (2004) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1695 , Issue.1-3 , pp. 3-17
    • Ciechanover, A.1    Schwartz, A.L.2
  • 112
    • 0038066613 scopus 로고    scopus 로고
    • The role of the ubiquitination-proteasome pathway in breast cancer. Ubiquitin mediated degradation of growth factor receptors in the pathogenesis and treatment of cancer
    • DOI 10.1186/bcr541
    • Lipkowitz S. The role of the ubiquitination-proteasome pathway in breast cancer: ubiquitin mediated degradation of growth factor receptors in the pathogenesis and treatment of cancer. Breast Cancer Res 2003; 5: 8-15. (Pubitemid 36553572)
    • (2003) Breast Cancer Research , vol.5 , Issue.1 , pp. 8-15
    • Lipkowitz, S.1
  • 113
    • 77449103325 scopus 로고    scopus 로고
    • Therapeutic strategies within the ubiquitin proteasome system
    • Eldridge AG, O'Brien T. Therapeutic strategies within the ubiquitin proteasome system. Cell Death Differ 2010; 17: 4-13.
    • (2010) Cell Death Differ , vol.17 , pp. 4-13
    • Eldridge, A.G.1    O'Brien, T.2
  • 114
    • 78650824534 scopus 로고    scopus 로고
    • Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets
    • Bedford L, Lowe J, Dick LR, Mayer RJ, Brownell JE. Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets. Nat Rev Drug Discov 2011; 10: 29-46.
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 29-46
    • Bedford, L.1    Lowe, J.2    Dick, L.R.3    Mayer, R.J.4    Brownell, J.E.5
  • 115
    • 38449099679 scopus 로고    scopus 로고
    • Role of proteasomes in disease
    • Dahlmann B. Role of proteasomes in disease. BMC Biochem 2007; 8(Suppl 1): S3.
    • (2007) BMC Biochem , vol.8 , Issue.SUPPL. 1
    • Dahlmann, B.1
  • 116
    • 77958056316 scopus 로고    scopus 로고
    • A proteasome inhibitor, bortezomib, inhibits breast cancer growth and reduces osteolysis by downregulating metastatic genes
    • Jones MD, Liu JC, Barthel TK, Hussain S, Lovria E, Cheng D et al. A proteasome inhibitor, bortezomib, inhibits breast cancer growth and reduces osteolysis by downregulating metastatic genes. Clin Cancer Res 2010; 16: 4978-4989.
    • (2010) Clin Cancer Res , vol.16 , pp. 4978-4989
    • Jones, M.D.1    Liu, J.C.2    Barthel, T.K.3    Hussain, S.4    Lovria, E.5    Cheng, D.6
  • 117
  • 118
    • 80052069445 scopus 로고    scopus 로고
    • Rings of good and evil: Ring finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis
    • Lipkowitz S, Weissman AM. RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis. Nat Rev Cancer 2011; 11: 629-643.
    • (2011) Nat Rev Cancer , vol.11 , pp. 629-643
    • Lipkowitz, S.1    Weissman, A.M.2
  • 119
    • 78049315806 scopus 로고    scopus 로고
    • Ubiquitin becomes ubiquitous in cancer: Emerging roles of ubiquitin ligases and deubiquitinases in tumorigenesis and as therapeutic targets
    • Shi D, Grossman SR. Ubiquitin becomes ubiquitous in cancer: emerging roles of ubiquitin ligases and deubiquitinases in tumorigenesis and as therapeutic targets. Cancer Biol Ther 2010; 10: 737-747.
    • (2010) Cancer Biol Ther , vol.10 , pp. 737-747
    • Shi, D.1    Grossman, S.R.2
  • 120
    • 77449137856 scopus 로고    scopus 로고
    • Roles of e3 ubiquitin ligases in cell adhesion and migration
    • Huang C. Roles of E3 ubiquitin ligases in cell adhesion and migration. Cell Adh Migr 2010; 4: 10-18.
    • (2010) Cell Adh Migr , vol.4 , pp. 10-18
    • Huang, C.1
  • 121
    • 77953768742 scopus 로고    scopus 로고
    • Cbl and human myeloid neoplasms: The cbl oncogene comes of age
    • Kales SC, Ryan PE, Nau MM, Lipkowitz S. Cbl and human myeloid neoplasms: the Cbl oncogene comes of age. Cancer Res 2010; 70: 4789-4794.
    • (2010) Cancer Res , vol.70 , pp. 4789-4794
    • Kales, S.C.1    Ryan, P.E.2    Nau, M.M.3    Lipkowitz, S.4
  • 122
    • 0038386452 scopus 로고    scopus 로고
    • Escape from Cbl-mediated downregulation: A recurrent theme for oncogenic deregulation of receptor tyrosine kinases
    • DOI 10.1016/S1535-6108(03)00136-3
    • Peschard P, Park M. Escape from Cbl-mediated downregulation: a recurrent theme for oncogenic deregulation of receptor tyrosine kinases. Cancer Cell 2003; 3: 519-523. (Pubitemid 36808646)
    • (2003) Cancer Cell , vol.3 , Issue.6 , pp. 519-523
    • Peschard, P.1    Park, M.2
  • 123
    • 77952479240 scopus 로고    scopus 로고
    • Cbl is frequently altered in lung cancers: Its relationship to mutations in met and egfr tyrosine kinases
    • Tan YH, Krishnaswamy S, Nandi S, Kanteti R, Vora S, Onel K et al. CBL is frequently altered in lung cancers: its relationship to mutations in MET and EGFR tyrosine kinases. PLoS One 2010; 5: e8972.
    • (2010) PLoS One , vol.5
    • Tan, Y.H.1    Krishnaswamy, S.2    Nandi, S.3    Kanteti, R.4    Vora, S.5    Onel, K.6
  • 124
    • 84871244194 scopus 로고    scopus 로고
    • Cbl enhances breast tumor formation by inhibiting tumor suppressive activity of tgf-beta signaling
    • Kang JM, Park S, Kim SJ, Hong HY, Jeong J, Kim HS. CBL enhances breast tumor formation by inhibiting tumor suppressive activity of TGF-beta signaling. Oncogene 2012; 31: 5123-5131.
    • (2012) Oncogene , vol.31 , pp. 5123-5131
    • Kang, J.M.1    Park, S.2    Kim, S.J.3    Hong, H.Y.4    Jeong, J.5    Kim, H.S.6
  • 125
    • 81755172038 scopus 로고    scopus 로고
    • An e3 ubiquitin ligase: C-cbl: A new therapeutic target of lung cancer
    • Lo FY, Tan YH, Cheng HC, Salgia R, Wang YC. An E3 ubiquitin ligase: c-Cbl: a new therapeutic target of lung cancer. Cancer 2011; 117: 5344-5350.
    • (2011) Cancer , vol.117 , pp. 5344-5350
    • Lo, F.Y.1    Tan, Y.H.2    Cheng, H.C.3    Salgia, R.4    Wang, Y.C.5
  • 126
    • 3543035771 scopus 로고    scopus 로고
    • Biology and therapeutic advances for pediatric osteosarcoma
    • DOI 10.1634/theoncologist.9-4-422
    • Marina N, Gebhardt M, Teot L, Gorlick R. Biology and therapeutic advances for pediatric osteosarcoma. Oncologist 2004; 9: 422-441. (Pubitemid 39014554)
    • (2004) Oncologist , vol.9 , Issue.4 , pp. 422-441
    • Marina, N.1    Gebhardt, M.2    Teot, L.3    Gorlick, R.4
  • 130
    • 70449727683 scopus 로고    scopus 로고
    • Runx2, p53, and prb status as diagnostic parameters for deregulation of osteoblast growth and differentiation in a new pre-chemotherapeutic osteosarcoma cell line (os1)
    • Pereira BP, Zhou Y, Gupta A, Leong DT, Aung KZ, Ling L et al. Runx2, p53, and pRB status as diagnostic parameters for deregulation of osteoblast growth and differentiation in a new pre-chemotherapeutic osteosarcoma cell line (OS1). J Cell Physiol 2009; 221: 778-788.
    • (2009) J Cell Physiol , vol.221 , pp. 778-788
    • Pereira, B.P.1    Zhou, Y.2    Gupta, A.3    Leong, D.T.4    Aung, K.Z.5    Ling, L.6
  • 131
    • 84863139254 scopus 로고    scopus 로고
    • Genomic promoter occupancy of runt-related transcription factor runx2 in osteosarcoma cells identifies genes involved in cell adhesion and motility
    • van der Deen M, Akech J, Lapointe D, Gupta S, Young DW, Montecino MA et al. Genomic promoter occupancy of runt-related transcription factor RUNX2 in osteosarcoma cells identifies genes involved in cell adhesion and motility. J Biol Chem 2012; 287: 4503-4517.
    • (2012) J Biol Chem , vol.287 , pp. 4503-4517
    • Van Der Deen, M.1    Akech, J.2    Lapointe, D.3    Gupta, S.4    Young, D.W.5    Montecino, M.A.6
  • 132
    • 33846034921 scopus 로고    scopus 로고
    • Regulatory roles of Runx2 in metastatic tumor and cancer cell interactions with bone
    • DOI 10.1007/s10555-006-9032-0, Special issue on Bone Metastasis and Cancer
    • Pratap J, Lian JB, Javed A, Barnes GL, van Wijnen AJ, Stein JL et al. Regulatory roles of Runx2 in metastatic tumor and cancer cell interactions with bone. Cancer Metastasis Rev 2006; 25: 589-600. (Pubitemid 46071865)
    • (2006) Cancer and Metastasis Reviews , vol.25 , Issue.4 , pp. 589-600
    • Pratap, J.1    Lian, J.B.2    Javed, A.3    Barnes, G.L.4    Van Wijnen, A.J.5    Stein, J.L.6    Stein, G.S.7
  • 133
    • 77953364958 scopus 로고    scopus 로고
    • Proteasome inhibition with bortezomib suppresses growth and induces apoptosis in osteosarcoma
    • Shapovalov Y, Benavidez D, Zuch D, Eliseev RA. Proteasome inhibition with bortezomib suppresses growth and induces apoptosis in osteosarcoma. Int J Cancer 2010; 127: 67-76.
    • (2010) Int J Cancer , vol.127 , pp. 67-76
    • Shapovalov, Y.1    Benavidez, D.2    Zuch, D.3    Eliseev, R.A.4
  • 135
    • 84866668120 scopus 로고    scopus 로고
    • Targeting the e3 ubiquitin casitas b-lineage lymphoma decreases osteosarcoma cell growth and survival and reduces tumorigenesis
    • Sévére N, Dieudonné FX, Marty C, Modrowski D, Patino-Garcia A, Lecanda F et al. Targeting the E3 ubiquitin casitas B-lineage lymphoma decreases osteosarcoma cell growth and survival and reduces tumorigenesis. J Bone Miner Res 2012; 27: 2108-2117.
    • (2012) J Bone Miner Res , vol.27 , pp. 2108-2117
    • Sévé Re, N.1    Dieudonné, F.X.2    Marty, C.3    Modrowski, D.4    Patino-Garcia, A.5    Lecanda, F.6
  • 136
    • 83255188851 scopus 로고    scopus 로고
    • Targeting of insulin-like growth factor type 1 receptor in ewing sarcoma: Unfulfilled promise or a promising beginning?
    • Ho AL, Schwartz GK. Targeting of insulin-like growth factor type 1 receptor in Ewing sarcoma: unfulfilled promise or a promising beginning? J Clin Oncol 2011; 29: 4581-4583.
    • (2011) J Clin Oncol , vol.29 , pp. 4581-4583
    • Ho, A.L.1    Schwartz, G.K.2
  • 137
    • 78650824534 scopus 로고    scopus 로고
    • Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets
    • Bedford L, Lowe J, Dick LR, Mayer RJ, Brownell JE. Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets. Nat Rev Drug Discov 2011; 10: 29-46.
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 29-46
    • Bedford, L.1    Lowe, J.2    Dick, L.R.3    Mayer, R.J.4    Brownell, J.E.5
  • 138
    • 77951757948 scopus 로고    scopus 로고
    • Erbb2 trafficking and degradation associated with k48 and k63 polyubiquitination
    • Marx C, Held JM, Gibson BW, Benz CC. ErbB2 trafficking and degradation associated with K48 and K63 polyubiquitination. Cancer Res 2010; 70: 3709-3717.
    • (2010) Cancer Res , vol.70 , pp. 3709-3717
    • Marx, C.1    Held, J.M.2    Gibson, B.W.3    Benz, C.C.4
  • 139
    • 80052919716 scopus 로고    scopus 로고
    • Usp1 deubiquitinates id proteins to preserve a mesenchymal stem cell program in osteosarcoma
    • Williams SA, Maecker HL, French DM, Liu J, Gregg A, Silverstein LB et al. USP1 deubiquitinates ID proteins to preserve a mesenchymal stem cell program in osteosarcoma. Cell 2011; 146: 918-930.
    • (2011) Cell , vol.146 , pp. 918-930
    • Williams, S.A.1    Maecker, H.L.2    French, D.M.3    Liu, J.4    Gregg, A.5    Silverstein, L.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.