메뉴 건너뛰기




Volumn 316, Issue 1, 2006, Pages 403-409

Erythropoietin receptor signal transduction requires protein geranylgeranylation

Author keywords

[No Author keywords available]

Indexed keywords

ERYTHROPOIETIN RECEPTOR; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; JANUS KINASE; MEVINOLIN;

EID: 29244482539     PISSN: 00223565     EISSN: 15210103     Source Type: Journal    
DOI: 10.1124/jpet.105.092510     Document Type: Article
Times cited : (7)

References (40)
  • 1
    • 0037129306 scopus 로고    scopus 로고
    • Rac is activated by erythropoietin or interleukin-3 and is involved in activation of the Erk signaling pathway
    • Arai A, Kanda E, and Miura O (2002) Rac is activated by erythropoietin or interleukin-3 and is involved in activation of the Erk signaling pathway. Oncogene 21:2641-2651.
    • (2002) Oncogene , vol.21 , pp. 2641-2651
    • Arai, A.1    Kanda, E.2    Miura, O.3
  • 2
    • 0034644537 scopus 로고    scopus 로고
    • Ras and Rho GTPases: A family reunion
    • Bar-Sagi D and Hall A (2000) Ras and Rho GTPases: a family reunion. Cell 103:227-238.
    • (2000) Cell , vol.103 , pp. 227-238
    • Bar-Sagi, D.1    Hall, A.2
  • 3
    • 0019857850 scopus 로고
    • Relationship of dolichol synthesis to glycoprotein synthesis during embryonic development
    • Carson DD and Lennarz WJ (1981) Relationship of dolichol synthesis to glycoprotein synthesis during embryonic development. J Biol Chem 256:4679-4686.
    • (1981) J Biol Chem , vol.256 , pp. 4679-4686
    • Carson, D.D.1    Lennarz, W.J.2
  • 4
    • 0027050783 scopus 로고
    • Biochemistry of protein prenylation
    • Casey PJ (1992) Biochemistry of protein prenylation. J Lipid Res 33:1731-1740.
    • (1992) J Lipid Res , vol.33 , pp. 1731-1740
    • Casey, P.J.1
  • 5
    • 0028957913 scopus 로고
    • Mechanisms of protein prenylation and role in G protein function
    • Casey PJ (1995) Mechanisms of protein prenylation and role in G protein function. Biochem Soc Trans 23:161-166.
    • (1995) Biochem Soc Trans , vol.23 , pp. 161-166
    • Casey, P.J.1
  • 6
    • 3042794598 scopus 로고    scopus 로고
    • Erythropoietin regulation of Raf-1 and MEK: Evidence for a Ras-independent mechanism
    • Chen C and Sytkowski AJ (2004) Erythropoietin regulation of Raf-1 and MEK: evidence for a Ras-independent mechanism. Blood 104:73-80.
    • (2004) Blood , vol.104 , pp. 73-80
    • Chen, C.1    Sytkowski, A.J.2
  • 7
    • 0027360189 scopus 로고
    • Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-kDa tyrosine-phosphorylated protein
    • Damen JE, Liu L, Cutler RL, and Krystal G (1993) Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-kDa tyrosine-phosphorylated protein. Blood 82:2296-2303.
    • (1993) Blood , vol.82 , pp. 2296-2303
    • Damen, J.E.1    Liu, L.2    Cutler, R.L.3    Krystal, G.4
  • 8
    • 0028785893 scopus 로고
    • Tyrosine 343 in the erythropoietin receptor positively regulates erythropoietin-induced cell proliferation and Stat5 activation
    • Damen JE, Wakao H, Miyajima A, Krosl J, Humphries RK, Cutler RL, and Krystal G (1995) Tyrosine 343 in the erythropoietin receptor positively regulates erythropoietin-induced cell proliferation and Stat5 activation. EMBO (Eur Mol Biol Organ) J 14:5557-5568.
    • (1995) EMBO (Eur Mol Biol Organ) J , vol.14 , pp. 5557-5568
    • Damen, J.E.1    Wakao, H.2    Miyajima, A.3    Krosl, J.4    Humphries, R.K.5    Cutler, R.L.6    Krystal, G.7
  • 9
    • 0033392946 scopus 로고    scopus 로고
    • Enzymology and biology of CaaX protein prenylation
    • Fu HW and Casey PJ (1999) Enzymology and biology of CaaX protein prenylation. Recent Prog Horm Res 54:313-342.
    • (1999) Recent Prog Horm Res , vol.54 , pp. 313-342
    • Fu, H.W.1    Casey, P.J.2
  • 10
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein JL and Brown MS (1990) Regulation of the mevalonate pathway. Nature (Lond) 343:425-430.
    • (1990) Nature (Lond) , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 11
    • 0036898609 scopus 로고    scopus 로고
    • RAC2 GTPase deficiency and myeloid cell dysfunction in human and mouse
    • Gu Y and Williams DA (2002) RAC2 GTPase deficiency and myeloid cell dysfunction in human and mouse. J Pediatr Hematol Oncol 24:791-794.
    • (2002) J Pediatr Hematol Oncol , vol.24 , pp. 791-794
    • Gu, Y.1    Williams, D.A.2
  • 12
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A (1998) Rho GTPases and the actin cytoskeleton. Science (Wash DC) 279:509-514.
    • (1998) Science (Wash DC) , vol.279 , pp. 509-514
    • Hall, A.1
  • 13
    • 0037155865 scopus 로고    scopus 로고
    • Consequences of mevalonate depletion. Differential transcriptional, translational, and post-translational upregulation of Ras, Rap1a, RhoA, and RhoB
    • Holstein SA, Wohlford-Lenane CL, and Hohl RJ (2002) Consequences of mevalonate depletion. Differential transcriptional, translational, and post-translational upregulation of Ras, Rap1a, RhoA, and RhoB. J Biol Chem 277:10678-10682.
    • (2002) J Biol Chem , vol.277 , pp. 10678-10682
    • Holstein, S.A.1    Wohlford-Lenane, C.L.2    Hohl, R.J.3
  • 14
    • 0025906597 scopus 로고
    • Post-translational modifications of the C-terminal region of the rho protein are important for its interaction with membranes and the stimulatory and inhibitory GDP/GTP exchange proteins
    • Hori Y, Kikuchi A, Isomura M, Katayama M, Miura Y, Fujioka H, Kaibuchi K, and Takai Y (1991) Post-translational modifications of the C-terminal region of the rho protein are important for its interaction with membranes and the stimulatory and inhibitory GDP/GTP exchange proteins. Oncogene 6:515-522.
    • (1991) Oncogene , vol.6 , pp. 515-522
    • Hori, Y.1    Kikuchi, A.2    Isomura, M.3    Katayama, M.4    Miura, Y.5    Fujioka, H.6    Kaibuchi, K.7    Takai, Y.8
  • 15
    • 0028800305 scopus 로고
    • Activation of Rac1, RhoA and mitogen-activated protein kinases is required for Ras transformation
    • Khosravi-Far R, Solski PA, Clark GJ, Kinch MS, and Der CJ (1995) Activation of Rac1, RhoA and mitogen-activated protein kinases is required for Ras transformation. Mol Cell Biol 15:6443-6453.
    • (1995) Mol Cell Biol , vol.15 , pp. 6443-6453
    • Khosravi-Far, R.1    Solski, P.A.2    Clark, G.J.3    Kinch, M.S.4    Der, C.J.5
  • 16
    • 0027049472 scopus 로고
    • The molecular mechanism of erythropoietin action
    • Koury MJ and Bondurant MC (1992) The molecular mechanism of erythropoietin action. Eur J Biochem 210:649-663.
    • (1992) Eur J Biochem , vol.210 , pp. 649-663
    • Koury, M.J.1    Bondurant, M.C.2
  • 17
    • 0026019106 scopus 로고
    • Erythropoietin
    • Krantz SB (1991) Erythropoietin. Blood 77:419-434.
    • (1991) Blood , vol.77 , pp. 419-434
    • Krantz, S.B.1
  • 18
    • 0024962490 scopus 로고
    • Protein modification: New clue to Ras lipid glue
    • Lowy DR and Willumsen BM (1989) Protein modification: new clue to Ras lipid glue. Nature (Lond) 341:384-385.
    • (1989) Nature (Lond) , vol.341 , pp. 384-385
    • Lowy, D.R.1    Willumsen, B.M.2
  • 19
    • 0032516846 scopus 로고    scopus 로고
    • Rho GTPases
    • Mackay DJ and Hall A (1998) Rho GTPases. J Biol Chem 273:20685-20688.
    • (1998) J Biol Chem , vol.273 , pp. 20685-20688
    • Mackay, D.J.1    Hall, A.2
  • 21
    • 0344011564 scopus 로고    scopus 로고
    • Epidermal growth factor receptor-targeted therapy potentiates lovastatin-induced apoptosis in head and neck squamous cell carcinoma cells
    • Mantha AJ, McFee KE, Niknejad N, Goss G, Lorimer IA, and Dimitroulakos J (2003) Epidermal growth factor receptor-targeted therapy potentiates lovastatin-induced apoptosis in head and neck squamous cell carcinoma cells. J Cancer Res Clin Oncol 129:631-641.
    • (2003) J Cancer Res Clin Oncol , vol.129 , pp. 631-641
    • Mantha, A.J.1    McFee, K.E.2    Niknejad, N.3    Goss, G.4    Lorimer, I.A.5    Dimitroulakos, J.6
  • 23
    • 0026806554 scopus 로고
    • Mammalian protein geranylgeranyltransferase. Subunit composition and metal requirements
    • Moomaw JF and Casey PJ (1992) Mammalian protein geranylgeranyltransferase. Subunit composition and metal requirements. J Biol Chem 267:17438-17443.
    • (1992) J Biol Chem , vol.267 , pp. 17438-17443
    • Moomaw, J.F.1    Casey, P.J.2
  • 24
    • 0033552910 scopus 로고    scopus 로고
    • Anti-apoptotic function of Rac in hematopoietic cells
    • Nishida K, Kaziro Y, and Satoh T (1999) Anti-apoptotic function of Rac in hematopoietic cells. Oncogene 18:407-415.
    • (1999) Oncogene , vol.18 , pp. 407-415
    • Nishida, K.1    Kaziro, Y.2    Satoh, T.3
  • 25
    • 0037313015 scopus 로고    scopus 로고
    • Rho family GTPases are required for activation of Jak/STAT signaling by G protein-coupled receptors
    • Pelletier S, Duhamel F, Coulombe P, Popoff MR, and Meloche S (2003) Rho family GTPases are required for activation of Jak/STAT signaling by G protein-coupled receptors. Mol Cell Biol 23:1316-1333.
    • (2003) Mol Cell Biol , vol.23 , pp. 1316-1333
    • Pelletier, S.1    Duhamel, F.2    Coulombe, P.3    Popoff, M.R.4    Meloche, S.5
  • 26
    • 0029598817 scopus 로고
    • Erythropoietin induces the tyrosine phosphorylation, nuclear translocation and DNA binding of STAT1 and STAT5 in erythroid cells
    • Penta K and Sawyer ST (1995) Erythropoietin induces the tyrosine phosphorylation, nuclear translocation and DNA binding of STAT1 and STAT5 in erythroid cells. J Biol Chem 270:31282-31287.
    • (1995) J Biol Chem , vol.270 , pp. 31282-31287
    • Penta, K.1    Sawyer, S.T.2
  • 28
    • 0029866781 scopus 로고    scopus 로고
    • Erythropoietin induces activation of Stat5 through association with specific tyrosines on the receptor that are not required for a mitogenic response
    • Quelle FW, Wang D, Nosaka T, Thierfelder WE, Stravopodis D, Weinstein Y, and Ihle JN (1996) Erythropoietin induces activation of Stat5 through association with specific tyrosines on the receptor that are not required for a mitogenic response. Mol Cell Biol 16:1622-1631.
    • (1996) Mol Cell Biol , vol.16 , pp. 1622-1631
    • Quelle, F.W.1    Wang, D.2    Nosaka, T.3    Thierfelder, W.E.4    Stravopodis, D.5    Weinstein, Y.6    Ihle, J.N.7
  • 29
    • 0030968859 scopus 로고    scopus 로고
    • Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo
    • Rowell CA, Kowalczyk JJ, Lewis MD, and Garcia AM (1997) Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo. J Biol Chem 272:14093-14097.
    • (1997) J Biol Chem , vol.272 , pp. 14093-14097
    • Rowell, C.A.1    Kowalczyk, J.J.2    Lewis, M.D.3    Garcia, A.M.4
  • 30
    • 0035844167 scopus 로고    scopus 로고
    • 3-Hydroxy-3-methylglutaryl-CoA reductase inhibitors block calcium-dependent tyrosine kinase Pyk2 activation by angiotensin II in vascular endothelial cells. Involvement of geranylgeranylation of small G protein Rap1
    • Satoh K, Ichihara K, Landon EJ, Inagami T, and Tang H (2001) 3-Hydroxy-3-methylglutaryl-CoA reductase inhibitors block calcium-dependent tyrosine kinase Pyk2 activation by angiotensin II in vascular endothelial cells. Involvement of geranylgeranylation of small G protein Rap1. J Biol Chem 276:15761-15767.
    • (2001) J Biol Chem , vol.276 , pp. 15761-15767
    • Satoh, K.1    Ichihara, K.2    Landon, E.J.3    Inagami, T.4    Tang, H.5
  • 32
    • 0034630098 scopus 로고    scopus 로고
    • Recent advances in the study of prenylated proteins
    • Sinensky M (2000) Recent advances in the study of prenylated proteins. Biochim Biophys Acta 1484:93-106.
    • (2000) Biochim Biophys Acta , vol.1484 , pp. 93-106
    • Sinensky, M.1
  • 34
    • 0026611269 scopus 로고
    • Erythropoietin induces p21ras activation and p120GAP tyrosine phosphorylation in human erythroleukemia cells
    • Torti M, Marti KB, Altschuler D, Yamamoto K, and Lapetina EG (1992) Erythropoietin induces p21ras activation and p120GAP tyrosine phosphorylation in human erythroleukemia cells. J Biol Chem 267:8293-8298.
    • (1992) J Biol Chem , vol.267 , pp. 8293-8298
    • Torti, M.1    Marti, K.B.2    Altschuler, D.3    Yamamoto, K.4    Lapetina, E.G.5
  • 35
    • 0142245593 scopus 로고    scopus 로고
    • Inhibition of protein geranylgeranylation induces apoptosis in myeloma plasma cells by reducing Mcl-1 protein levels
    • Van de Donk NW, Kamphuis MM, van Kessel B, Lokhorst HM, and Bloem AC (2003) Inhibition of protein geranylgeranylation induces apoptosis in myeloma plasma cells by reducing Mcl-1 protein levels. Blood 102:3354-3362.
    • (2003) Blood , vol.102 , pp. 3354-3362
    • Van De Donk, N.W.1    Kamphuis, M.M.2    Van Kessel, B.3    Lokhorst, H.M.4    Bloem, A.C.5
  • 36
    • 0027327484 scopus 로고
    • JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin
    • Witthuhn BA, Quelle FW, Silvennoinen O, Yi T, Tang B, Miura O, and Ihle JN (1993) JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin. Cell 74:227-236.
    • (1993) Cell , vol.74 , pp. 227-236
    • Witthuhn, B.A.1    Quelle, F.W.2    Silvennoinen, O.3    Yi, T.4    Tang, B.5    Miura, O.6    Ihle, J.N.7
  • 37
    • 0034857309 scopus 로고    scopus 로고
    • Blocking protein geranylgeranylation is essential for lovastatin-induced apoptosis of human acute myeloid leukemia cells
    • Xia Z, Tan MM, Wong WW, Dimitroulakos J, Minden MD, and Penn LZ (2001) Blocking protein geranylgeranylation is essential for lovastatin-induced apoptosis of human acute myeloid leukemia cells. Leukemia 15:1398-1407.
    • (2001) Leukemia , vol.15 , pp. 1398-1407
    • Xia, Z.1    Tan, M.M.2    Wong, W.W.3    Dimitroulakos, J.4    Minden, M.D.5    Penn, L.Z.6
  • 38
  • 39
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang FL and Casey PJ (1996) Protein prenylation: molecular mechanisms and functional consequences. Annu Rev Biochem 65:241-269.
    • (1996) Annu Rev Biochem , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 40
    • 0041920695 scopus 로고    scopus 로고
    • Lovastatin induces apoptosis of anaplastic thyroid cancer cells via inhibition of protein geranylgeranylation and de novo protein synthesis
    • Zhong WB, Wang CY, Chang TC, and Lee WS (2003) Lovastatin induces apoptosis of anaplastic thyroid cancer cells via inhibition of protein geranylgeranylation and de novo protein synthesis. Endocrinology 144:3852-3859.
    • (2003) Endocrinology , vol.144 , pp. 3852-3859
    • Zhong, W.B.1    Wang, C.Y.2    Chang, T.C.3    Lee, W.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.