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Volumn 3, Issue 1, 2008, Pages

A mitochondrial kinase complex is essential to mediate an ERK1/2-dependent phosphorylation of a key regulatory protein in steroid biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CHOLESTEROL; EPIDERMAL GROWTH FACTOR; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; OXYTETRACYCLINE; PROGESTERONE; SERINE; STEROID; STEROIDOGENIC ACUTE REGULATORY PROTEIN; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; PHOSPHOPROTEIN;

EID: 39049122124     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0001443     Document Type: Article
Times cited : (101)

References (62)
  • 1
    • 0019217650 scopus 로고
    • Intracellular movement of cholesterol in rat adrenal cells. Kinetics and effects of inhibitors
    • Crivello JF, Jefcoate CR (1980) Intracellular movement of cholesterol in rat adrenal cells. Kinetics and effects of inhibitors. J Biol Chem 255: 8144-8151.
    • (1980) J Biol Chem , vol.255 , pp. 8144-8151
    • Crivello, J.F.1    Jefcoate, C.R.2
  • 2
    • 0343807261 scopus 로고
    • Regulation of intramitochondrial cholesterol transfer to side-chain cleavage cytochrome P-450 in rat adrenal gland
    • Privalle CT, Crivello JF, Jefcoate CR (1983) Regulation of intramitochondrial cholesterol transfer to side-chain cleavage cytochrome P-450 in rat adrenal gland. Proc Natl Acad Sci U S A 80: 702-706.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 702-706
    • Privalle, C.T.1    Crivello, J.F.2    Jefcoate, C.R.3
  • 3
    • 0026591024 scopus 로고
    • Isolation of the mitochondrial benzodiazepine receptor: Association with the voltage-dependent anion channel and the adenine nucleotide, carrier
    • McEncry MW, Snowman AM, Trifiletti RR, Snyder SH (1992) Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide, carrier. Proc Natl Acad Sci U S A 89: 3170-3174.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 3170-3174
    • McEncry, M.W.1    Snowman, A.M.2    Trifiletti, R.R.3    Snyder, S.H.4
  • 4
    • 33746035655 scopus 로고    scopus 로고
    • Translocator protein (18 kDa): New nomenclature for the peripheral-type benzodiazepine receptor based on its structure and molecular function
    • Papadopoulos V, Baraldi M, Guilarte TR, Knudsen TB, Lacapere JJ, et al. (2006) Translocator protein (18 kDa): new nomenclature for the peripheral-type benzodiazepine receptor based on its structure and molecular function. Trends Pharmacol Sci 27: 402-409.
    • (2006) Trends Pharmacol Sci , vol.27 , pp. 402-409
    • Papadopoulos, V.1    Baraldi, M.2    Guilarte, T.R.3    Knudsen, T.B.4    Lacapere, J.J.5
  • 5
    • 33845977384 scopus 로고    scopus 로고
    • Protein-Protein Interactions Mediate Mitochondrial Cholesterol Transport and Steroid Biosynthesis
    • Liu J, Rone MB, Papadopoulos V (2006) Protein-Protein Interactions Mediate Mitochondrial Cholesterol Transport and Steroid Biosynthesis. J Biol Chem 281: 38879-38893.
    • (2006) J Biol Chem , vol.281 , pp. 38879-38893
    • Liu, J.1    Rone, M.B.2    Papadopoulos, V.3
  • 6
    • 0028104418 scopus 로고
    • The purification, cloning, and expression of a novel luteinizing hormone-induced mitochondrial protein in MA-10 mouse Leydig tumor cells. Characterization of die steroidogenic acute regulatory protein (StAR)
    • Clark BJ, Wells J, King SR, Stocco DM (1994) The purification, cloning, and expression of a novel luteinizing hormone-induced mitochondrial protein in MA-10 mouse Leydig tumor cells. Characterization of die steroidogenic acute regulatory protein (StAR). J Biol Chem 269. 28314-28322.
    • (1994) J Biol Chem , vol.269 , pp. 28314-28322
    • Clark, B.J.1    Wells, J.2    King, S.R.3    Stocco, D.M.4
  • 7
    • 0037007628 scopus 로고    scopus 로고
    • Rapid regulation of steroidogenesis by mitochondrial protein impom
    • Bose H, Lingappa VR, Miller WL (2002) Rapid regulation of steroidogenesis by mitochondrial protein impom Nature 417: 87-91.
    • (2002) Nature , vol.417 , pp. 87-91
    • Bose, H.1    Lingappa, V.R.2    Miller, W.L.3
  • 8
    • 0020636067 scopus 로고
    • Acute adrenocorticotropic hormone stimulation of adrenal corticosteroidogenesis. Discovery of a rapidly induced protein
    • Krueger RJ, Orme-Johnson NR (1983) Acute adrenocorticotropic hormone stimulation of adrenal corticosteroidogenesis. Discovery of a rapidly induced protein. J Biol Chem 258: 10159-10167.
    • (1983) J Biol Chem , vol.258 , pp. 10159-10167
    • Krueger, R.J.1    Orme-Johnson, N.R.2
  • 9
    • 0025941096 scopus 로고
    • The 30-kDa mitochondrial proteins induced by hormone stimulation in MA-10 mouse Leydig tumor cells are processed from larger precursors
    • Stocco DM, Sodeman TC (1991) The 30-kDa mitochondrial proteins induced by hormone stimulation in MA-10 mouse Leydig tumor cells are processed from larger precursors. J Biol Chem 266: 19731-19738.
    • (1991) J Biol Chem , vol.266 , pp. 19731-19738
    • Stocco, D.M.1    Sodeman, T.C.2
  • 10
    • 33749595667 scopus 로고    scopus 로고
    • Mitochondrial processing of bovine adrenal steroidogenic acute regulatory protein
    • Yamazaki T, Matsuoka C, Gendou M, Izumi S, Zhao D, et al. (2006) Mitochondrial processing of bovine adrenal steroidogenic acute regulatory protein. Biochim Biophys Acta 1764: 1561-1567.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1561-1567
    • Yamazaki, T.1    Matsuoka, C.2    Gendou, M.3    Izumi, S.4    Zhao, D.5
  • 11
    • 0025996448 scopus 로고
    • Regulation of steroid hormone biosynthesis. Identification of precursors of a phosphoprotein targeted to the mitochondrion in stimulated rat adrenal cortex cells
    • Epstein LF, Orme-Johnson NR (1991) Regulation of steroid hormone biosynthesis. Identification of precursors of a phosphoprotein targeted to the mitochondrion in stimulated rat adrenal cortex cells. J Biol Chem 266: 19739-19745.
    • (1991) J Biol Chem , vol.266 , pp. 19739-19745
    • Epstein, L.F.1    Orme-Johnson, N.R.2
  • 12
    • 33847041060 scopus 로고    scopus 로고
    • Mechanism ofStAR's regulation of mitochondrial cholesterol import
    • Miller WL (2007) Mechanism ofStAR's regulation of mitochondrial cholesterol import. Mol Cell Endocrinol 265-266: 46-50.
    • (2007) Mol Cell Endocrinol , vol.265-266 , pp. 46-50
    • Miller, W.L.1
  • 13
    • 0030459652 scopus 로고    scopus 로고
    • Steroidogenic, acute regulatory protein (StAR) retains activity in the absence of its mitochondrial import sequence: Implications for the mechanism of StAR action
    • Arakane F, Sugawara T, Niahino H, Liu Z, Holt JA, et al. (1996) Steroidogenic, acute regulatory protein (StAR) retains activity in the absence of its mitochondrial import sequence: implications for the mechanism of StAR action. Proc Natl Acad Sci U S A 93: 13731-13736.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 13731-13736
    • Arakane, F.1    Sugawara, T.2    Niahino, H.3    Liu, Z.4    Holt, J.A.5
  • 14
    • 0033133729 scopus 로고    scopus 로고
    • Soltys BJ, Gupta RS (1999) Mitochondrial-matrix proteins at unexpected locations: are they exported? Trends Biochern Sci 24: 174-177.
    • Soltys BJ, Gupta RS (1999) Mitochondrial-matrix proteins at unexpected locations: are they exported? Trends Biochern Sci 24: 174-177.
  • 15
    • 0035824668 scopus 로고    scopus 로고
    • Mitochondrial processing of newly synthesized steroidogcnic acute regulatory protein (StAR), but not total StAR, mediates cholesterol transfer to cytochrome P450 side chain cleavage enzyme in adrenal cells
    • Artemenko IP, Zhao D, Hales DB, Hales KH, Jefcoate CR (2001) Mitochondrial processing of newly synthesized steroidogcnic acute regulatory protein (StAR), but not total StAR, mediates cholesterol transfer to cytochrome P450 side chain cleavage enzyme in adrenal cells. J Biol Chem 276: 46583-46596.
    • (2001) J Biol Chem , vol.276 , pp. 46583-46596
    • Artemenko, I.P.1    Zhao, D.2    Hales, D.B.3    Hales, K.H.4    Jefcoate, C.R.5
  • 16
    • 33746084479 scopus 로고    scopus 로고
    • Energized, Polarized, and Actively Respiring Mitochondria Are Required for Acute Leydig Cell Steroidogenesis
    • Allen JA, Shankara T, Janus P, Buck S, Dierner T, et al. (2006) Energized, Polarized, and Actively Respiring Mitochondria Are Required for Acute Leydig Cell Steroidogenesis. Endocrinology 147: 3924-3935.
    • (2006) Endocrinology , vol.147 , pp. 3924-3935
    • Allen, J.A.1    Shankara, T.2    Janus, P.3    Buck, S.4    Dierner, T.5
  • 17
    • 34547679741 scopus 로고    scopus 로고
    • An arachidonic acid generation/export system involved in the regulation of cholesterol transport in mitochondria of steroidogenic cells
    • Duarte A, Castillo AF, Castilla R, Maloberti P, Paz C, et al. (2007) An arachidonic acid generation/export system involved in the regulation of cholesterol transport in mitochondria of steroidogenic cells. Febs Letters 581: 4023-4028.
    • (2007) Febs Letters , vol.581 , pp. 4023-4028
    • Duarte, A.1    Castillo, A.F.2    Castilla, R.3    Maloberti, P.4    Paz, C.5
  • 18
    • 0031730449 scopus 로고    scopus 로고
    • Effect of truncated forms of the steroidogenic acute regulatory protein on intramitochondrial cholesterol transfer
    • Wang X, Liu Z, Eimerl S, Timberg R, Weiss AM, et al. (1998) Effect of truncated forms of the steroidogenic acute regulatory protein on intramitochondrial cholesterol transfer. Endocrinology 139: 3903-3912.
    • (1998) Endocrinology , vol.139 , pp. 3903-3912
    • Wang, X.1    Liu, Z.2    Eimerl, S.3    Timberg, R.4    Weiss, A.M.5
  • 19
    • 0030047248 scopus 로고    scopus 로고
    • Regulation of the acute production of steroids in steroidogenic cells
    • Stocco DM, Clark BJ (1996) Regulation of the acute production of steroids in steroidogenic cells. Endocr Rev 17: 221-244.
    • (1996) Endocr Rev , vol.17 , pp. 221-244
    • Stocco, D.M.1    Clark, B.J.2
  • 20
    • 27644505023 scopus 로고    scopus 로고
    • Multiple signaling pathways regulating steroidogenesis and steroidogenic acute regulatory protein expression: More complicated than we thought
    • Stocco DM, Wang X, Jo Y, Manna PR (2005) Multiple signaling pathways regulating steroidogenesis and steroidogenic acute regulatory protein expression: more complicated than we thought Mol Endocrirol 19: 2647-2659.
    • (2005) Mol Endocrirol , vol.19 , pp. 2647-2659
    • Stocco, D.M.1    Wang, X.2    Jo, Y.3    Manna, P.R.4
  • 21
    • 4444287241 scopus 로고    scopus 로고
    • Phosphorylation and function of the hamster adrenal steroidogenic acute regulatory protein (StAR)
    • Fleury A, Mathieu A.P, Ducharme L, Hales DB, LeHoux JG (2004) Phosphorylation and function of the hamster adrenal steroidogenic acute regulatory protein (StAR). J Steroid Biochem Mol Biol 91: 259-271.
    • (2004) J Steroid Biochem Mol Biol , vol.91 , pp. 259-271
    • Fleury, A.1    Mathieu, A.P.2    Ducharme, L.3    Hales, D.B.4    LeHoux, J.G.5
  • 22
    • 0020315854 scopus 로고
    • Compartmentalization of corticotropin-dependent steroidogenic factors in adrenal cortex: Evidence for a post-translational cascade in stimulation of the cholesterol side-chain split
    • Neher R, Milani A, Solano AR, Poaesta EJ (1982) Compartmentalization of corticotropin-dependent steroidogenic factors in adrenal cortex: evidence for a post-translational cascade in stimulation of the cholesterol side-chain split. Proc Natl Acad Sci U S A 79: 1727-1731.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 1727-1731
    • Neher, R.1    Milani, A.2    Solano, A.R.3    Poaesta, E.J.4
  • 23
    • 0017104245 scopus 로고
    • Adenosine 3′,5′-monophosphate-dependent protein kinase of Leydig cells: In vitro activation and relationship to gonadotropin action upon cyclic AMP and steroidogenesis
    • Podesta EJ, Dufau ML, Catt KJ (1976) Adenosine 3′,5′-monophosphate-dependent protein kinase of Leydig cells: in vitro activation and relationship to gonadotropin action upon cyclic AMP and steroidogenesis. FEBS Lett 70: 212-216.
    • (1976) FEBS Lett , vol.70 , pp. 212-216
    • Podesta, E.J.1    Dufau, M.L.2    Catt, K.J.3
  • 24
    • 0018422131 scopus 로고
    • Adrenocorticotropin artion in isolated adrenal cells. The intermediate role of cyclic AMP in stimulation of corticosterone synthcsis
    • Sala GB, Hayashi K, Catt KJ, Dufau ML (1979) Adrenocorticotropin artion in isolated adrenal cells. The intermediate role of cyclic AMP in stimulation of corticosterone synthcsis. J Biol Chem 234: 3861-3865.
    • (1979) J Biol Chem , vol.234 , pp. 3861-3865
    • Sala, G.B.1    Hayashi, K.2    Catt, K.J.3    Dufau, M.L.4
  • 25
    • 0018749073 scopus 로고
    • Mutations in cyclic AMP-dependent protein kinase and corticotropin (ACTH)-sensitive adenylate cyclase affect adrenal steroidogenesis
    • Rae PA, Gutmann NS, Tsao J, Schimmer BP (1979) Mutations in cyclic AMP-dependent protein kinase and corticotropin (ACTH)-sensitive adenylate cyclase affect adrenal steroidogenesis. Proc Natl Acad Sci U S A 76: 1896-1900.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 1896-1900
    • Rae, P.A.1    Gutmann, N.S.2    Tsao, J.3    Schimmer, B.P.4
  • 26
    • 0017181858 scopus 로고
    • Correlation of protein kinase activation and testosterone production after stimulation of Leydig cells with luteinizing hormone
    • Cooke BA, Lindh ML, Janszen FH (1976) Correlation of protein kinase activation and testosterone production after stimulation of Leydig cells with luteinizing hormone. Biochem J 160: 439-446.
    • (1976) Biochem J , vol.160 , pp. 439-446
    • Cooke, B.A.1    Lindh, M.L.2    Janszen, F.H.3
  • 27
    • 0035860761 scopus 로고    scopus 로고
    • ERKs regulate cyclic AMP-induced steroid synthesis through transcription of the steroidogenic acute regulatory (StAR) gene
    • Gyles SL, Burns CJ, Whitehouse BJ, Sugden D, Marsh FJ, et al. (2001) ERKs regulate cyclic AMP-induced steroid synthesis through transcription of the steroidogenic acute regulatory (StAR) gene.J Biol Chem 276: 34888-34895.
    • (2001) J Biol Chem , vol.276 , pp. 34888-34895
    • Gyles, S.L.1    Burns, C.J.2    Whitehouse, B.J.3    Sugden, D.4    Marsh, F.J.5
  • 28
    • 0242298720 scopus 로고    scopus 로고
    • The lutropin/choriogonadotropin receptor-induced phosphorylation of the extracellular signal-regulated kinases in leydig cells is mediated by a protein kinase a-dependent activation of ras
    • Hirakawa T, Ascoli M (2003) The lutropin/choriogonadotropin receptor-induced phosphorylation of the extracellular signal-regulated kinases in leydig cells is mediated by a protein kinase a-dependent activation of ras. Mol Endocrinol 17: 2189-2200.
    • (2003) Mol Endocrinol , vol.17 , pp. 2189-2200
    • Hirakawa, T.1    Ascoli, M.2
  • 29
    • 34247377842 scopus 로고    scopus 로고
    • Regulation of Leydig cell steroidogenesis by extracellular signal-regulated kinase 1/2: Role of protein kinase A and protein kinase C signaling
    • Manna PR, Jo Y, Stocco DM (2007) Regulation of Leydig cell steroidogenesis by extracellular signal-regulated kinase 1/2: role of protein kinase A and protein kinase C signaling. J Endocrinol 193: 53-63.
    • (2007) J Endocrinol , vol.193 , pp. 53-63
    • Manna, P.R.1    Jo, Y.2    Stocco, D.M.3
  • 30
    • 4644293240 scopus 로고    scopus 로고
    • Extracellular Signal-Regulated Kinases Are Involved in the Acute Activation of Steroidogenesis in Immature Rat Leydig Cells by Human Chononic Gonadotropin
    • Martinelle N, Holst M, Soder O, Svechnikov K (2004) Extracellular Signal-Regulated Kinases Are Involved in the Acute Activation of Steroidogenesis in Immature Rat Leydig Cells by Human Chononic Gonadotropin. Endocrinology 145: 4629-4634.
    • (2004) Endocrinology , vol.145 , pp. 4629-4634
    • Martinelle, N.1    Holst, M.2    Soder, O.3    Svechnikov, K.4
  • 31
    • 0035958046 scopus 로고    scopus 로고
    • The ERK Signaling Cascade Inhibits Gonadotropin-stimulated Steroidogenesis
    • Seger R, Hanoch T, Rosenberg R, Dantes A, Metz WE, et al. (2001) The ERK Signaling Cascade Inhibits Gonadotropin-stimulated Steroidogenesis. J Biol Chem 276: 13957-13964.
    • (2001) J Biol Chem , vol.276 , pp. 13957-13964
    • Seger, R.1    Hanoch, T.2    Rosenberg, R.3    Dantes, A.4    Metz, W.E.5
  • 32
    • 33847053928 scopus 로고    scopus 로고
    • Role of MAPKs in angiotensin II-induced steroidogenesis in rat glomerulosa cells
    • Otis M, Gallo-Payet N (2007) Role of MAPKs in angiotensin II-induced steroidogenesis in rat glomerulosa cells. Mol Cell Endocrinol 265 266: 126-130.
    • (2007) Mol Cell Endocrinol , vol.265 , Issue.266 , pp. 126-130
    • Otis, M.1    Gallo-Payet, N.2
  • 33
    • 0037040343 scopus 로고    scopus 로고
    • Mitochondrial PKCepsilon and MAPK form signaling modules in the murine heart: Enhanced mitochondrial PKCepsilon-MAPK interactions and differential MAPK activation in PKCepsilon-induced cardioprotection
    • Baines CP, Zhang J, Wang GW, Zheng YT, Yiu JX, et al. (2002) Mitochondrial PKCepsilon and MAPK form signaling modules in the murine heart: enhanced mitochondrial PKCepsilon-MAPK interactions and differential MAPK activation in PKCepsilon-induced cardioprotection. Circ Res 90: 390-397.
    • (2002) Circ Res , vol.90 , pp. 390-397
    • Baines, C.P.1    Zhang, J.2    Wang, G.W.3    Zheng, Y.T.4    Yiu, J.X.5
  • 34
    • 1842562333 scopus 로고    scopus 로고
    • Mitochondrial extracellular signal-regulated kinases 1/2 (ERK1/2) are modulated during brain development
    • Alonso M, Melani M, Converso D, Jaitovich A, Paz C, et al. (2004) Mitochondrial extracellular signal-regulated kinases 1/2 (ERK1/2) are modulated during brain development. J Neurochem 89: 248-256.
    • (2004) J Neurochem , vol.89 , pp. 248-256
    • Alonso, M.1    Melani, M.2    Converso, D.3    Jaitovich, A.4    Paz, C.5
  • 35
    • 0034527424 scopus 로고    scopus 로고
    • A role for the p42/44 isoforms of MAPK in the regulation of steroid secretion from Y1 mouse adrenocortical cells
    • Gyles SL, Burns CJ, Persaud SJ, Jones PM, Whitehouse BJ (2000) A role for the p42/44 isoforms of MAPK in the regulation of steroid secretion from Y1 mouse adrenocortical cells. Endocr Res 26: 579-581.
    • (2000) Endocr Res , vol.26 , pp. 579-581
    • Gyles, S.L.1    Burns, C.J.2    Persaud, S.J.3    Jones, P.M.4    Whitehouse, B.J.5
  • 36
    • 33646153064 scopus 로고    scopus 로고
    • Induction of steroidogenesis in immature rat Leydig cells by interleukin-1alpha is dependent on extracellular signal-regulated kinases
    • Renlund N, Jo Y, Svechnikova I, Holst M, Stocco DM, et al. (2006) Induction of steroidogenesis in immature rat Leydig cells by interleukin-1alpha is dependent on extracellular signal-regulated kinases. J Mol Endocrinol 36: 327-336.
    • (2006) J Mol Endocrinol , vol.36 , pp. 327-336
    • Renlund, N.1    Jo, Y.2    Svechnikova, I.3    Holst, M.4    Stocco, D.M.5
  • 37
    • 17144420535 scopus 로고    scopus 로고
    • Silencing the expression of mitochondrial acyl-CoA thioesterase I and acyl-CoA synthetase 4 inhibits hormone-induced steroidogenesis
    • Maloberti P, Castilla R, Castillo F, Maciel FC, Mendez CF, et al. (2005) Silencing the expression of mitochondrial acyl-CoA thioesterase I and acyl-CoA synthetase 4 inhibits hormone-induced steroidogenesis. Febs J 272: 180-1814.
    • (2005) Febs J , vol.272 , pp. 180-1814
    • Maloberti, P.1    Castilla, R.2    Castillo, F.3    Maciel, F.C.4    Mendez, C.F.5
  • 38
    • 33745167984 scopus 로고    scopus 로고
    • Activation of the lutropin/ choriogonadotropin receptor in MA-10 cells stimulates tyrosine kinase cascades that activate ras and the extracellular signal regulated kinases (ERK1I/2)
    • Shiraishi K, Ascoli M (2006) Activation of the lutropin/ choriogonadotropin receptor in MA-10 cells stimulates tyrosine kinase cascades that activate ras and the extracellular signal regulated kinases (ERK1I/2). Endocrinology 147: 3419-3427.
    • (2006) Endocrinology , vol.147 , pp. 3419-3427
    • Shiraishi, K.1    Ascoli, M.2
  • 39
    • 0037177819 scopus 로고    scopus 로고
    • Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1
    • Robinson FL, Whitehurst AW, Raman M, Cobb MH (2002) Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1. J Biol Chem 277: 1484-14852.
    • (2002) J Biol Chem , vol.277 , pp. 1484-14852
    • Robinson, F.L.1    Whitehurst, A.W.2    Raman, M.3    Cobb, M.H.4
  • 40
    • 0023240362 scopus 로고
    • Epidermal growth factor activates steroid biosynthesis in cultured Leydig tumor cells without affecting the levels of cAMP and potentiates the activation of steroid biosynthesis by choriogonadotropin and cAMP
    • Ascoli M, Euffa J, Segaloff DL (1987) Epidermal growth factor activates steroid biosynthesis in cultured Leydig tumor cells without affecting the levels of cAMP and potentiates the activation of steroid biosynthesis by choriogonadotropin and cAMP. J Biol Chem 262: 9196-9203.
    • (1987) J Biol Chem , vol.262 , pp. 9196-9203
    • Ascoli, M.1    Euffa, J.2    Segaloff, D.L.3
  • 41
    • 33750563633 scopus 로고    scopus 로고
    • cAMP increases mitochondrial cholesterol transport through the induction of arachidonic acid release inside this organelle in MA-10 Leydig cells
    • Castillo F, Cornejo Maciel F, Castilla R, Duarte A, Maloberti P, et al. (2006) cAMP increases mitochondrial cholesterol transport through the induction of arachidonic acid release inside this organelle in MA-10 Leydig cells. Febs J 273: 5011-5021.
    • (2006) Febs J , vol.273 , pp. 5011-5021
    • Castillo, F.1    Cornejo Maciel, F.2    Castilla, R.3    Duarte, A.4    Maloberti, P.5
  • 42
    • 0027296646 scopus 로고
    • Molecular cloning, expression, and characterization of the human mitogen-activated protein kinase p44ewrkl
    • Charest DL, Mordret G, Harder KW, Jirik F, Pelech SL (1993) Molecular cloning, expression, and characterization of the human mitogen-activated protein kinase p44ewrkl. Mol Cell Biol 13: 4679-4690.
    • (1993) Mol Cell Biol , vol.13 , pp. 4679-4690
    • Charest, D.L.1    Mordret, G.2    Harder, K.W.3    Jirik, F.4    Pelech, S.L.5
  • 43
    • 0029821204 scopus 로고    scopus 로고
    • Methods and reagents. Purification of GST fusion proteins
    • Hengen PN (1996) Methods and reagents. Purification of GST fusion proteins. Trends Biochem Sci 21: 400-401.
    • (1996) Trends Biochem Sci , vol.21 , pp. 400-401
    • Hengen, P.N.1
  • 45
    • 33744798469 scopus 로고    scopus 로고
    • Docking interactions induce exposure of activation loop in the MAP kinase ERK2
    • Zhou T, Sun L, Humphreys J, Goldsmith EJ (2006) Docking interactions induce exposure of activation loop in the MAP kinase ERK2. Structure 14: 1011-1019.
    • (2006) Structure , vol.14 , pp. 1011-1019
    • Zhou, T.1    Sun, L.2    Humphreys, J.3    Goldsmith, E.J.4
  • 46
    • 0035854672 scopus 로고    scopus 로고
    • Hydrophobic as well as charged residues in both MEK1 and ERK2 are important for their proper docking
    • Xu B, Stippec S, Robinson FL, Cobb MH (2001) Hydrophobic as well as charged residues in both MEK1 and ERK2 are important for their proper docking. J Biol Chem 276: 26509-26515.
    • (2001) J Biol Chem , vol.276 , pp. 26509-26515
    • Xu, B.1    Stippec, S.2    Robinson, F.L.3    Cobb, M.H.4
  • 47
    • 0025888298 scopus 로고
    • Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases
    • Gonzalez FA, Raden DL, Davis RJ (1991) Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases. J Biol Chem 266: 22159-22163.
    • (1991) J Biol Chem , vol.266 , pp. 22159-22163
    • Gonzalez, F.A.1    Raden, D.L.2    Davis, R.J.3
  • 48
    • 0037444809 scopus 로고    scopus 로고
    • Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity
    • Bardwell AJ, Abdollahi M, Bardwell L (2003) Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity. Biochem J 370: 1077-1085.
    • (2003) Biochem J , vol.370 , pp. 1077-1085
    • Bardwell, A.J.1    Abdollahi, M.2    Bardwell, L.3
  • 49
    • 0035920179 scopus 로고    scopus 로고
    • Docking sites on substrate proteins direct extracellular signal-regulated kinase to phosphorylate specific residues
    • Fantz DA, Jacobs D, Glossip D, Kornfeld K (2001) Docking sites on substrate proteins direct extracellular signal-regulated kinase to phosphorylate specific residues. J Biol Chem 276: 27256-27265.
    • (2001) J Biol Chem , vol.276 , pp. 27256-27265
    • Fantz, D.A.1    Jacobs, D.2    Glossip, D.3    Kornfeld, K.4
  • 50
    • 33847235315 scopus 로고    scopus 로고
    • StAR search-what we know about bow the steroidogenic acute regulatory protein mediates mitochondrial cholesterol import
    • Miller WL (2007) StAR search-what we know about bow the steroidogenic acute regulatory protein mediates mitochondrial cholesterol import. Mol Endocrinol 21: 589-601.
    • (2007) Mol Endocrinol , vol.21 , pp. 589-601
    • Miller, W.L.1
  • 51
    • 0035813102 scopus 로고    scopus 로고
    • Steroidogenic acute regulatory protein binds cholesterol and modulates mitochondrial membrane sterol domain dynamics
    • Petrescu AD, Gallegos AM, Okamura Y, Strauss JF 3rd, Schroeder F (2001) Steroidogenic acute regulatory protein binds cholesterol and modulates mitochondrial membrane sterol domain dynamics. J Biol Chem 276: 36970-36982.
    • (2001) J Biol Chem , vol.276 , pp. 36970-36982
    • Petrescu, A.D.1    Gallegos, A.M.2    Okamura, Y.3    Strauss 3rd, J.F.4    Schroeder, F.5
  • 53
    • 0036436915 scopus 로고    scopus 로고
    • Concerted regulation of free arachidonic acid and hormone-induced steroid synthesis by acyl-CoA thioesterases and acyl-CoA synthetases in adrenal cells
    • Maloberti P, Lozano RC, Mele PG, Cano F, Colonna C, et al. (2002) Concerted regulation of free arachidonic acid and hormone-induced steroid synthesis by acyl-CoA thioesterases and acyl-CoA synthetases in adrenal cells. Eur J Biochem 269: 5599-5607.
    • (2002) Eur J Biochem , vol.269 , pp. 5599-5607
    • Maloberti, P.1    Lozano, R.C.2    Mele, P.G.3    Cano, F.4    Colonna, C.5
  • 54
    • 0019364734 scopus 로고
    • Characterization of several clonal lines of cultured Leyelig tumor cells: Gonadotropin receptors and steroidogenic responses
    • Ascoli M (1981) Characterization of several clonal lines of cultured Leyelig tumor cells: gonadotropin receptors and steroidogenic responses. Endocrinology 108: 88-95.
    • (1981) Endocrinology , vol.108 , pp. 88-95
    • Ascoli, M.1
  • 55
    • 2442768285 scopus 로고
    • Adrenocorticotropin (ACTH) induces phosphorylation of a cytoplasmic protein in intact isolated adrenocortical cells
    • Podesta EJ, Milani A, Stefren H, Neher R (1979) Adrenocorticotropin (ACTH) induces phosphorylation of a cytoplasmic protein in intact isolated adrenocortical cells. Proc Natl Acad Sci U S A 76: 5187-5191.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 5187-5191
    • Podesta, E.J.1    Milani, A.2    Stefren, H.3    Neher, R.4
  • 56
    • 0020771654 scopus 로고
    • Rapid, quantitative isolation of mitochondria from rat liver using Yicoll gradients in vertical rotors
    • Stocco DM (1983) Rapid, quantitative isolation of mitochondria from rat liver using Yicoll gradients in vertical rotors. Anal Biochem 131: 453-457.
    • (1983) Anal Biochem , vol.131 , pp. 453-457
    • Stocco, D.M.1
  • 57
    • 0031453141 scopus 로고    scopus 로고
    • Phosphorylation of steroidogenic acute regulatory protein (StAR) modulates its steroidogenic activity
    • Arakane F, King SR, Du Y, Kallen CB, Walsh LP, et al. (1997) Phosphorylation of steroidogenic acute regulatory protein (StAR) modulates its steroidogenic activity. J Biol Chem 272: 32656-32662.
    • (1997) J Biol Chem , vol.272 , pp. 32656-32662
    • Arakane, F.1    King2    SR, D.Y.3    Kallen, C.B.4    Walsh, L.P.5
  • 58
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc, Natl Acad Sci U S A 76: 4350-4354.
    • (1979) Proc, Natl Acad Sci U S A , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 59
    • 14644401125 scopus 로고    scopus 로고
    • ACTH-induced caveolin-1 tyrosine phosphorylation is related to podosome assembly in Yl adrenal cells
    • Colonna C, Podesta EJ (2005) ACTH-induced caveolin-1 tyrosine phosphorylation is related to podosome assembly in Yl adrenal cells. Exp Cell Res 304: 432-02.
    • (2005) Exp Cell Res , vol.304 , pp. 432-502
    • Colonna, C.1    Podesta, E.J.2
  • 60
    • 0034888034 scopus 로고    scopus 로고
    • LH/ chorionic gonadotropin signaling pathway involves protein tyrosine phosphatase activity downstream of protein kinase A activation: Evidence of an obligatory step in steroid production by Leydig cells
    • Cornejo Maciel F, Poderoso C, Gorostizaga A, Paz C, Podesta EJ (2001) LH/ chorionic gonadotropin signaling pathway involves protein tyrosine phosphatase activity downstream of protein kinase A activation: evidence of an obligatory step in steroid production by Leydig cells. J Endocrinol 170: 403-411.
    • (2001) J Endocrinol , vol.170 , pp. 403-411
    • Cornejo Maciel, F.1    Poderoso, C.2    Gorostizaga, A.3    Paz, C.4    Podesta, E.J.5
  • 61
    • 0036932676 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases are involved in LH/chorionic gonadotropin and 8Br-cAMP regulation of steroidogenesis and StAR protein levels in MA-10 leydig cells
    • Paz C, Cornejo Maciel. F, Maloberti P, Walsh LP, Stocco DM, et al. (2002) Protein tyrosine phosphatases are involved in LH/chorionic gonadotropin and 8Br-cAMP regulation of steroidogenesis and StAR protein levels in MA-10 leydig cells. J Endocrinol 175: 793-801.
    • (2002) J Endocrinol , vol.175 , pp. 793-801
    • Paz, C.1    Cornejo Maciel, F.2    Maloberti, P.3    Walsh, L.P.4    Stocco, D.M.5
  • 62
    • 0023472472 scopus 로고
    • Tricine-sodium, dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von Jagow G (1987) Tricine-sodium, dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166: 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2


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