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Volumn 287, Issue 19, 2012, Pages 15380-15394

Hormone-induced 14-3-3γ adaptor protein regulates steroidogenic acute regulatory protein activity and steroid biosynthesis in MA-10 leydig cells

Author keywords

[No Author keywords available]

Indexed keywords

14-3-3 PROTEINS; ADAPTOR PROTEINS; BINDING MOTIF; CYTOSOLIC; DE NOVO SYNTHESIS; HOMODIMERIZATION; HUMAN CHORIONIC GONADOTROPINS; IMMUNOBLOTTING; IMMUNOPRECIPITATIONS; INNER MITOCHONDRIAL MEMBRANES; LEYDIG CELLS; LIPID TRANSFER; MITOCHONDRIAL COMPLEX; OUTER MITOCHONDRIAL MEMBRANES; PROTEIN COMPLEXES; RATE-LIMITING STEPS; STEROID BIOSYNTHESIS; STEROID HORMONE; STEROIDOGENIC ACUTE REGULATORY PROTEINS; TARGET PROTEINS;

EID: 84860866704     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.339580     Document Type: Article
Times cited : (42)

References (68)
  • 1
    • 0030047248 scopus 로고    scopus 로고
    • Regulation of the acute production of steroids in steroidogenic cells
    • DOI 10.1210/er.17.3.221
    • Stocco, D. M., and Clark, B. J. (1996) Regulation of the acute production of steroids in steroidogenic cells. Endocr. Rev. 17, 221-244 (Pubitemid 26001082)
    • (1996) Endocrine Reviews , vol.17 , Issue.3 , pp. 221-244
    • Stocco, D.M.1    Clark, B.J.2
  • 2
  • 3
    • 0022966989 scopus 로고
    • Acute stimulation of steroidogenesis in corpus luteum and adrenal cortex by peptide hormones. Rapid induction of a similar protein in both tissues
    • Pon, L. A., and Orme-Johnson, N. R. (1986) Acute stimulation of steroid-ogenesis in corpus luteum and adrenal cortex by peptide hormones. Rapid induction of a similar protein in both tissues. J. Biol. Chem. 261, 6594-6599 (Pubitemid 17204178)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.14 , pp. 6594-6599
    • Pon, L.A.1    Orme-Johnson, N.2
  • 4
    • 33847039156 scopus 로고    scopus 로고
    • Is there a mitochondrial signaling complex facilitating cholesterol import?
    • DOI 10.1016/j.mce.2006.12.004, PII S0303720706005594, Adrenal/Molecular Steroidogenesis Conference 2006 AMS 2006
    • Papadopoulos, V., Liu, J., and Culty, M. (2007) Is there a mitochondrial signaling complex facilitating cholesterol import? Mol. Cell. Endocrinol. 265, 59-64 (Pubitemid 46273951)
    • (2007) Molecular and Cellular Endocrinology , vol.265-266 , Issue.SUPPL. , pp. 59-64
    • Papadopoulos, V.1    Liu, J.2    Culty, M.3
  • 5
    • 67649288976 scopus 로고    scopus 로고
    • Cholesterol transport in steroid biosynthesis. Role of protein-protein interactions and implications in disease states
    • Rone, M. B., Fan, J., and Papadopoulos, V. (2009) Cholesterol transport in steroid biosynthesis. Role of protein-protein interactions and implications in disease states. Biochim. Biophys. Acta 1791, 646-658
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 646-658
    • Rone, M.B.1    Fan, J.2    Papadopoulos, V.3
  • 6
    • 67651210634 scopus 로고    scopus 로고
    • Targeting and insertion of the cholesterol binding translocator protein into the outer mitochondrial membrane
    • Rone, M. B., Liu, J., Blonder, J., Ye, X., Veenstra, T. D., Young, J. C., and Papadopoulos, V. (2009) Targeting and insertion of the cholesterol binding translocator protein into the outer mitochondrial membrane. Biochemistry 48, 6909-6920
    • (2009) Biochemistry , vol.48 , pp. 6909-6920
    • Rone, M.B.1    Liu, J.2    Blonder, J.3    Ye, X.4    Veenstra, T.D.5    Young, J.C.6    Papadopoulos, V.7
  • 7
    • 0345643393 scopus 로고    scopus 로고
    • Cyclic-AMP-dependent protein kinase (PKA) in testicular cells. Cell specific expression, differential regulation and targeting of subunits of PKA
    • DOI 10.1016/S0960-0760(99)00077-1, PII S0960076099000771
    • Hansson, V., Skålhegg, B. S., and Taskén, K. (1999) Cyclic-AMP-dependent protein kinase (PKA) in testicular cells. Cell-specific expression, differential regulation, and targeting of subunits of PKA. J. Steroid Biochem. Mol. Biol. 69, 367-378 (Pubitemid 29305558)
    • (1999) Journal of Steroid Biochemistry and Molecular Biology , vol.69 , Issue.1-6 , pp. 367-378
    • Hansson, V.1    Skalhegg, B.S.2    Tasken, K.3
  • 8
    • 0035207765 scopus 로고    scopus 로고
    • Identification, localization, and function in steroidogenesis of PAP7: A peripheral-type benzodiazepine receptor- and PKA (RIα)-associated protein
    • DOI 10.1210/me.15.12.2211
    • Li, H., Degenhardt, B., Tobin, D., Yao, Z. X., Tasken, K., and Papadopoulos, V. (2001) Identification, localization, and function in steroidogenesis of PAP7. A peripheral-type benzodiazepine receptor- and PKA (RIα)-associated protein. Mol. Endocrinol. 15, 2211-2228 (Pubitemid 33141139)
    • (2001) Molecular Endocrinology , vol.15 , Issue.12 , pp. 2211-2228
    • Li, H.1    Degenhardt, B.2    Tobin, D.3    Yao, Z.-X.4    Tasken, K.5    Papadopoulos, V.6
  • 9
    • 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 the steroidogenic acute regulatory protein (StAR)
    • Clark, B. J., Wells, J., King, S. R., and Stocco, D. M. (1994) The purification, cloning, and expression of a novel luteinizing hormone-induced mitochondrial protein in MA-10 mouse Leydig tumor cells. Characterization of the 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
  • 11
    • 0032428003 scopus 로고    scopus 로고
    • Steroidogenic acute regulatory protein (StAR) acts on the outside of mitochondria to stimulate steroidogenesis
    • Arakane, F., Kallen, C. B., Watari, H., Stayrook, S. E., Lewis, M., and Strauss, J. F., 3rd (1998) Steroidogenic acute regulatory protein (StAR) acts on the outside of mitochondria to stimulate steroidogenesis. Endocr. Res. 24, 463-468 (Pubitemid 29016426)
    • (1998) Endocrine Research , vol.24 , Issue.3-4 , pp. 463-468
    • Arakane, F.1    Kallen, C.B.2    Watari, H.3    Stayrook, S.E.4    Lewis, M.5    Strauss III, J.F.6
  • 12
    • 0032566935 scopus 로고    scopus 로고
    • Unveiling the mechanism of action and regulation of the steroidogenic acute regulatory protein
    • DOI 10.1016/S0303-7207(98)00167-1, PII S0303720798001671
    • Kallen, C. B., Arakane, F., Christenson, L. K., Watari, H., Devoto, L., and Strauss, J. F., 3rd (1998) Unveiling the mechanism of action and regulation of the steroidogenic acute regulatory protein. Mol. Cell. Endocrinol. 145, 39-45 (Pubitemid 29003175)
    • (1998) Molecular and Cellular Endocrinology , vol.145 , Issue.1-2 , pp. 39-45
    • Kallen, C.B.1    Arakane, F.2    Christenson, L.K.3    Watari, H.4    Devoto, L.5    Strauss III, J.F.6
  • 13
    • 0037033098 scopus 로고    scopus 로고
    • Transfer of cholesterol between phospholipid vesicles mediated by the steroidogenic acute regulatory protein (StAR)
    • DOI 10.1074/jbc.M206965200
    • Tuckey, R. C., Headlam, M. J., Bose, H. S., and Miller, W. L. (2002) Transfer of cholesterol between phospholipid vesicles mediated by the steroidogenic acute regulatory protein (StAR). J. Biol. Chem. 277, 47123-47128 (Pubitemid 36159221)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.49 , pp. 47123-47128
    • Tuckey, R.C.1    Headlam, M.J.2    Bose, H.S.3    Miller, W.L.4
  • 14
    • 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, L. F., and Orme-Johnson, N. R. (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 (Pubitemid 21908289)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.29 , pp. 19739-19745
    • Epstein, L.F.1    Orme-Johnson, N.R.2
  • 15
    • 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, D. M., and Sodeman, T. C. (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 (Pubitemid 21908288)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.29 , pp. 19731-19738
    • Stocco, D.M.1    Sodeman, T.C.2
  • 17
    • 38549180522 scopus 로고    scopus 로고
    • Mitochondrial A-kinase anchoring protein 121 binds type II protein kinase A and enhances steroidogenic acute regulatory protein-mediated steroidogenesis in MA-10 mouse Leydig tumor cells
    • DOI 10.1095/biolreprod.107.064238
    • Dyson, M. T., Jones, J. K., Kowalewski, M. P., Manna, P. R., Alonso, M., Gottesman, M. E., and Stocco, D. M. (2008) Mitochondrial A kinase anchoring protein 121 binds type II protein kinase A and enhances steroidogenic acute regulatory protein-mediated steroidogenesis in MA-10 mouse Leydig tumor cells. Biol. Reprod. 78, 267-277 (Pubitemid 351159982)
    • (2008) Biology of Reproduction , vol.78 , Issue.2 , pp. 267-277
    • Dyson, M.T.1    Jones, J.K.2    Kowalewski, M.P.3    Manna, P.R.4    Alonso, M.5    Gottesman, M.E.6    Stocco, D.M.7
  • 18
    • 22544470581 scopus 로고    scopus 로고
    • Involvement of protein kinase C and cyclic adenosine 3′,5′- monophosphate-dependent kinase in steroidogenic acute regulatory protein expression and steroid biosynthesis in Leydig cells
    • DOI 10.1095/biolreprod.104.037721
    • Jo, Y., King, S. R., Khan, S. A., and Stocco, D. M. (2005) Involvement of protein kinase C and cyclic adenosine 3',5'-monophosphate-dependent kinase in steroidogenic acute regulatory protein expression and steroid biosynthesis in Leydig cells. Biol. Reprod. 73, 244-255 (Pubitemid 41022783)
    • (2005) Biology of Reproduction , vol.73 , Issue.2 , pp. 244-255
    • Jo, Y.1    King, S.R.2    Khan, S.A.3    Stocco, D.M.4
  • 19
    • 4444287241 scopus 로고    scopus 로고
    • Phosphorylation and function of the hamster adrenal steroidogenic acute regulatory protein (StAR)
    • DOI 10.1016/j.jsbmb.2004.04.010, PII S0960076004002900
    • Fleury, A., Mathieu, A. P., Ducharme, L., Hales, D. B., and LeHoux, J. G. (2004) Phosphorylation and function of the hamster adrenal steroidogenic acute regulatory protein (StAR). J. Steroid Biochem. Mol. Biol. 91, 259-271 (Pubitemid 39164608)
    • (2004) Journal of Steroid Biochemistry and Molecular Biology , vol.91 , Issue.4-5 , pp. 259-271
    • Fleury, A.1    Mathieu, A.P.2    Ducharme, L.3    Hales, D.B.4    Lehoux, J.-G.5
  • 20
    • 44049097217 scopus 로고    scopus 로고
    • Steroidogenic activity of StAR requires contact with mitochondrial VDAC1 and phosphate carrier protein
    • Bose, M., Whittal, R. M., Miller, W. L., and Bose, H. S. (2008) Steroidogenic activity of StAR requires contact with mitochondrial VDAC1 and phosphate carrier protein. J. Biol. Chem. 283, 8837-8845
    • (2008) J. Biol. Chem. , vol.283 , pp. 8837-8845
    • Bose, M.1    Whittal, R.M.2    Miller, W.L.3    Bose, H.S.4
  • 21
    • 0029147913 scopus 로고
    • Hormonal and developmental regulation of the steroidogenic acute regulatory protein
    • Clark, B. J., Soo, S. C., Caron, K. M., Ikeda, Y., Parker, K. L., and Stocco, D. M. (1995) Hormonal and developmental regulation of the steroidogenic acute regulatory protein. Mol. Endocrinol. 9, 1346-1355
    • (1995) Mol. Endocrinol. , vol.9 , pp. 1346-1355
    • Clark, B.J.1    Soo, S.C.2    Caron, K.M.3    Ikeda, Y.4    Parker, K.L.5    Stocco, D.M.6
  • 23
    • 29244448021 scopus 로고    scopus 로고
    • A pH-dependent molten globule transition is required for activity of the steroidogenic acute regulatory protein, StAR
    • DOI 10.1074/jbc.M510241200
    • Baker, B. Y., Yaworsky, D. C., and Miller, W. L. (2005) A pH-dependent molten globule transition is required for activity of the steroidogenic acute regulatory protein, StAR. J. Biol. Chem. 280, 41753-41760 (Pubitemid 41832238)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.50 , pp. 41753-41760
    • Baker, B.Y.1    Yaworsky, D.C.2    Miller, W.L.3
  • 25
    • 0037007628 scopus 로고    scopus 로고
    • Rapid regulation of steroidogenesis by mitochondrial protein import
    • DOI 10.1038/417087a
    • Bose, H. S., Lingappa, V. R., and Miller, W. L. (2002) Rapid regulation of steroidogenesis by mitochondrial protein import. Nature 417, 87-91 (Pubitemid 34498821)
    • (2002) Nature , vol.417 , Issue.6884 , pp. 87-91
    • Bose, H.S.1    Lingappat, V.R.2    Miller, W.L.3
  • 26
    • 34249811452 scopus 로고    scopus 로고
    • Cholesterol binding does not predict activity of the steroidogenic acute regulatory protein, StAR
    • DOI 10.1074/jbc.M611221200
    • Baker, B. Y., Epand, R. F., Epand, R. M., and Miller, W. L. (2007) Cholesterol binding does not predict activity of the steroidogenic acute regulatory protein, StAR. J. Biol. Chem. 282, 10223-10232 (Pubitemid 47093431)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.14 , pp. 10223-10232
    • Baker, B.Y.1    Epand, R.F.2    Epand, R.M.3    Miller, W.L.4
  • 27
    • 0028819993 scopus 로고
    • Structure of the human steroidogenic acute regulatory protein (StAR) gene. StAR stimulates mitochondrial cholesterol 27-hydroxylase activity
    • Sugawara, T., Lin, D., Holt, J. A., Martin, K. O., Javitt, N. B., Miller, W. L., and Strauss, J. F., 3rd (1995) Structure of the human steroidogenic acute regulatory protein (StAR) gene. StAR stimulates mitochondrial cholesterol 27-hydroxylase activity. Biochemistry 34, 12506-12512
    • (1995) Biochemistry , vol.34 , pp. 12506-12512
    • Sugawara, T.1    Lin, D.2    Holt, J.A.3    Martin, K.O.4    Javitt, N.B.5    Miller, W.L.6    Strauss III, J.F.7
  • 28
    • 0038683275 scopus 로고    scopus 로고
    • Transcriptional regulation of the mouse steroidogenic acute regulatory protein gene by the cAMP respose-element binding protein and steroidogenic factor 1
    • DOI 10.1677/jme.0.0300381
    • Manna, P. R., Eubank, D. W., Lalli, E., Sassone-Corsi, P., and Stocco, D. M. (2003) Transcriptional regulation of the mouse steroidogenic acute regulatory protein gene by the cAMP response element-binding protein and steroidogenic factor 1. J. Mol. Endocrinol. 30, 381-397 (Pubitemid 36722626)
    • (2003) Journal of Molecular Endocrinology , vol.30 , Issue.3 , pp. 381-397
    • Manna, P.R.1    Eubank, D.W.2    Lalli, E.3    Sassone-Corsi, P.4    Stocco, D.M.5
  • 30
    • 0034064138 scopus 로고    scopus 로고
    • Structure and lipid transport mechanism of a StAr-related domain
    • DOI 10.1038/75192
    • Tsujishita, Y., and Hurley, J. H. (2000) Structure and lipid transport mechanism of a StAR-related domain. Nat. Struct. Biol. 7, 408-414 (Pubitemid 30250006)
    • (2000) Nature Structural Biology , vol.7 , Issue.5 , pp. 408-414
    • Tsujishita, Y.1    Hurley, J.H.2
  • 31
    • 0034522555 scopus 로고    scopus 로고
    • Floundering about at cell membranes: A structural view of phospholipid signaling
    • DOI 10.1016/S0959-440X(00)00144-5
    • Hurley, J. H., Tsujishita, Y., and Pearson, M. A. (2000) Floundering about at cell membranes. A structural view of phospholipid signaling. Curr. Opin. Struct. Biol. 10, 737-743 (Pubitemid 32061490)
    • (2000) Current Opinion in Structural Biology , vol.10 , Issue.6 , pp. 737-743
    • Hurley, J.H.1    Tsujishita, Y.2    Pearson, M.A.3
  • 32
    • 0033719624 scopus 로고    scopus 로고
    • Evolution of the 14-3-3 protein family. Does the large number of isoforms in multicellular organisms reflect functional specificity?
    • Rosenquist, M., Sehnke, P., Ferl, R. J., Sommarin, M., and Larsson, C. (2000) Evolution of the 14-3-3 protein family. Does the large number of isoforms in multicellular organisms reflect functional specificity? J. Mol. Evol. 51, 446-458
    • (2000) J. Mol. Evol. , vol.51 , pp. 446-458
    • Rosenquist, M.1    Sehnke, P.2    Ferl, R.J.3    Sommarin, M.4    Larsson, C.5
  • 33
    • 0035473486 scopus 로고    scopus 로고
    • 14-3-3 Proteins; bringing new definitions to scaffolding
    • DOI 10.1038/sj.onc.1204777
    • Tzivion, G., Shen, Y. H., and Zhu, J. (2001) 14-3-3 proteins. Bringing new definitions to scaffolding. Oncogene 20, 6331-6338 (Pubitemid 32977842)
    • (2001) Oncogene , vol.20 , Issue.44 REV. ISS. 5 , pp. 6331-6338
    • Tzivion, G.1    Shen, Y.H.2    Zhu, J.3
  • 34
    • 33646926129 scopus 로고    scopus 로고
    • 14-3-3 Proteins.Ahistoric overview
    • Aitken, A. (2006) 14-3-3 proteins.Ahistoric overview. Semin. Cancer Biol. 16, 162-172
    • (2006) Semin. Cancer Biol. , vol.16 , pp. 162-172
    • Aitken, A.1
  • 35
    • 0027949375 scopus 로고
    • MSF, a novel cytoplasmic chaperone which functions in precursor targeting to mitochondria
    • Hachiya, N., Komiya, T., Alam, R., Iwahashi, J., Sakaguchi, M., Omura, T., and Mihara, K. (1994) MSF, a novel cytoplasmic chaperone that functions in precursor targeting to mitochondria. EMBO J. 13, 5146-5154 (Pubitemid 24341096)
    • (1994) EMBO Journal , vol.13 , Issue.21 , pp. 5146-5154
    • Hachiya, N.1    Komiya, T.2    Alam, R.3    Iwahashi, J.4    Sakaguchi, M.5    Omura, T.6    Mihara, K.7
  • 36
    • 0030811911 scopus 로고    scopus 로고
    • The 14-3-3 protein binds its target proteins with a common site located towards the C-terminus
    • DOI 10.1016/S0014-5793(97)00910-1, PII S0014579397009101
    • Ichimura, T., Ito, M., Itagaki, C., Takahashi, M., Horigome, T., Omata, S., Ohno, S., and Isobe, T. (1997) The 14-3-3 protein binds its target proteins with a common site located toward the C terminus. FEBS Lett. 413, 273-276 (Pubitemid 27353283)
    • (1997) FEBS Letters , vol.413 , Issue.2 , pp. 273-276
    • Ichimura, T.1    Ito, M.2    Itagaki, C.3    Takahashi, M.4    Horigome, T.5    Omata, S.6    Ohno, S.7    Isobe, T.8
  • 37
    • 0026539479 scopus 로고
    • Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) from sheep brain. Amino acid sequence of phosphorylated forms
    • Toker, A., Sellers, L. A., Amess, B., Patel, Y., Harris, A., and Aitken, A. (1992) Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) from sheep brain. Amino acid sequence of phosphorylated forms. Eur. J. Biochem. 206, 453-461
    • (1992) Eur. J. Biochem. , vol.206 , pp. 453-461
    • Toker, A.1    Sellers, L.A.2    Amess, B.3    Patel, Y.4    Harris, A.5    Aitken, A.6
  • 38
    • 0028979375 scopus 로고
    • Structure of a 14-3-3 protein and implications for coordination of multiple signaling pathways
    • Xiao, B., Smerdon, S. J., Jones, D. H., Dodson, G. G., Soneji, Y., Aitken, A., and Gamblin, S. J. (1995) Structure of a 14-3-3 protein and implications for coordination of multiple signaling pathways. Nature 376, 188-191
    • (1995) Nature , vol.376 , pp. 188-191
    • Xiao, B.1    Smerdon, S.J.2    Jones, D.H.3    Dodson, G.G.4    Soneji, Y.5    Aitken, A.6    Gamblin, S.J.7
  • 39
    • 0029046812 scopus 로고
    • Crystal structure of the ≲ζτα∀ isoform of the 14-3-3 protein
    • Liu, D., Bienkowska, J., Petosa, C., Collier, R. J., Fu, H., and Liddington, R. (1995) Crystal structure of the ≲ζτα∀ isoform of the 14-3-3 protein. Nature 376, 191-194
    • (1995) Nature , vol.376 , pp. 191-194
    • Liu, D.1    Bienkowska, J.2    Petosa, C.3    Collier, R.J.4    Fu, H.5    Liddington, R.6
  • 42
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • DOI 10.1016/S0092-8674(00)81067-3
    • Muslin, A. J., Tanner, J. W., Allen, P. M., and Shaw, A. S. (1996) Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84, 889-897 (Pubitemid 26106858)
    • (1996) Cell , vol.84 , Issue.6 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 43
    • 20844451376 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor-mediated action of steroidogenic acute regulatory protein on cholesterol entry into Leydig cell mitochondria
    • DOI 10.1210/me.2004-0307
    • Hauet, T., Yao, Z. X., Bose, H. S., Wall, C. T., Han, Z., Li, W., Hales, D. B., Miller, W. L., Culty, M., and Papadopoulos, V. (2005) Peripheral-type benzodiazepine receptor-mediated action of steroidogenic acute regulatory protein on cholesterol entry into Leydig cell mitochondria. Mol. Endocrinol. 19, 540-554 (Pubitemid 40223475)
    • (2005) Molecular Endocrinology , vol.19 , Issue.2 , pp. 540-554
    • Hauet, T.1    Yao, Z.-X.2    Bose, H.S.3    Wall, C.T.4    Han, Z.5    Li, W.6    Hales, D.B.7    Miller, W.L.8    Culty, M.9    Papadopoulos, V.10
  • 44
    • 0035970108 scopus 로고    scopus 로고
    • Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide
    • Li, H., Yao, Z., Degenhardt, B., Teper, G., and Papadopoulos, V. (2001) Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide. Proc. Natl. Acad. Sci. U.S.A. 98, 1267-1272
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1267-1272
    • Li, H.1    Yao, Z.2    Degenhardt, B.3    Teper, G.4    Papadopoulos, V.5
  • 46
    • 0036792481 scopus 로고    scopus 로고
    • High-flux mitochondrial cholesterol trafficking, a specialized function of the adrenal cortex
    • Jefcoate, C. (2002) High-flux mitochondrial cholesterol trafficking, a specialized function of the adrenal cortex. J. Clin. Invest. 110, 881-890
    • (2002) J. Clin. Invest. , vol.110 , pp. 881-890
    • Jefcoate, C.1
  • 47
    • 0042889456 scopus 로고    scopus 로고
    • PAP7, a PBR/PKA-RIα-associated protein: A new element in the relay of the hormonal induction of steroidogenesis
    • DOI 10.1016/S0960-0760(03)00213-9
    • Liu, J., Li, H., and Papadopoulos, V. (2003) PAP7, a PBR/PKA-RIα- associated protein. A new element in the relay of the hormonal induction of steroidogenesis. J. Steroid Biochem. Mol. Biol. 85, 275-283 (Pubitemid 37011103)
    • (2003) Journal of Steroid Biochemistry and Molecular Biology , vol.85 , Issue.2-5 , pp. 275-283
    • Liu, J.1    Li, H.2    Papadopoulos, V.3
  • 48
    • 33845977384 scopus 로고    scopus 로고
    • Protein-protein interactions mediate mitochondrial cholesterol transport and steroid biosynthesis
    • DOI 10.1074/jbc.M608820200
    • Liu, J., Rone, M. B., and Papadopoulos, V. (2006) Protein-protein interactions mediate mitochondrial cholesterol transport and steroid biosynthesis. J. Biol. Chem. 281, 38879-38893 (Pubitemid 46042015)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.50 , pp. 38879-38893
    • Liu, J.1    Rone, M.B.2    Papadopoulos, V.3
  • 49
    • 0032974109 scopus 로고    scopus 로고
    • Cytoplasmic localization of human cdc25C during interphase requires an intact 14-3-3 binding site
    • Dalal, S. N., Schweitzer, C. M., Gan, J., and DeCaprio, J. A. (1999) Cytoplasmic localization of human cdc25C during interphase requires an intact 14-3-3 binding site. Mol. Cell. Biol. 19, 4465-4479 (Pubitemid 29242020)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.6 , pp. 4465-4479
    • Dalal, S.N.1    Schweitzer, C.M.2    Gan, J.3    DeCaprio, J.A.4
  • 50
    • 0036893516 scopus 로고    scopus 로고
    • A novel heterodimerization domain, CRM1, and 14-3-3 control subcellular localization of the MondoA-Mlx heterocomplex
    • DOI 10.1128/MCB.22.24.8514-8526.2002
    • Eilers, A. L., Sundwall, E., Lin, M., Sullivan, A. A., and Ayer, D. E. (2002) A novel heterodimerization domain, CRM1, and 14-3-3 control subcellular localization of the MondoA-Mlx heterocomplex. Mol. Cell. Biol. 22, 8514-8526 (Pubitemid 35397167)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.24 , pp. 8514-8526
    • Eilers, A.L.1    Sundwall, E.2    Lin, M.3    Sullivan, A.A.4    Ayer, D.E.5
  • 51
    • 0037112527 scopus 로고    scopus 로고
    • 14-3-3 interacts with the tumor suppressor tuberin at Akt phosphorylation site(s)
    • Liu, M. Y., Cai, S., Espejo, A., Bedford, M. T., and Walker, C. L. (2002) 14-3-3 interacts with the tumor suppressor tuberin at Akt phosphorylation site(s). Cancer Res. 62, 6475-6480 (Pubitemid 35364110)
    • (2002) Cancer Research , vol.62 , Issue.22 , pp. 6475-6480
    • Liu, M.Y.1    Cai, S.2    Espejo, A.3    Bedford, M.T.4    Walker, C.L.5
  • 52
    • 79953142901 scopus 로고    scopus 로고
    • 14-3-3γ inhibition of MDMX-mediated p21 turnover independent of p53
    • Lee, J. H., and Lu, H. (2011) 14-3-3γ inhibition of MDMX-mediated p21 turnover independent of p53. J. Biol. Chem. 286, 5136-5142
    • (2011) J. Biol. Chem. , vol.286 , pp. 5136-5142
    • Lee, J.H.1    Lu, H.2
  • 53
    • 77955373300 scopus 로고    scopus 로고
    • 14-3-3γ induces oncogenic transformation by stimulatingMAPkinase and PI3K signaling
    • Radhakrishnan, V. M., and Martinez, J. D. (2010) 14-3-3γ induces oncogenic transformation by stimulatingMAPkinase and PI3K signaling. PLoS One 5, e11433
    • (2010) PLoS One , vol.5
    • Radhakrishnan, V.M.1    Martinez, J.D.2
  • 55
    • 33644877400 scopus 로고    scopus 로고
    • 14-3-3 Proteins. A number of functions for a numbered protein
    • Bridges, D., and Moorhead, G. B. (2005) 14-3-3 proteins. A number of functions for a numbered protein. Sci. STKE. 2005, re10
    • (2005) Sci. STKE. , vol.2005
    • Bridges, D.1    Moorhead, G.B.2
  • 56
    • 0026512368 scopus 로고
    • Endozepine/ diazepam binding inhibitor in adrenocortical and Leydig cell lines. Absence of hormonal regulation
    • Brown, A. S., Hall, P. F., Shoyab, M., and Papadopoulos, V. (1992) Endozepine/ diazepam binding inhibitor in adrenocortical and Leydig cell lines. Absence of hormonal regulation. Mol. Cell. Endocrinol. 83, 1-9
    • (1992) Mol. Cell. Endocrinol. , vol.83 , pp. 1-9
    • Brown, A.S.1    Hall, P.F.2    Shoyab, M.3    Papadopoulos, V.4
  • 57
    • 0036914288 scopus 로고    scopus 로고
    • Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants
    • Aitken, A. (2002) Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants. Plant Mol. Biol. 50, 993-1010
    • (2002) Plant Mol. Biol. , vol.50 , pp. 993-1010
    • Aitken, A.1
  • 59
    • 0345659206 scopus 로고    scopus 로고
    • Significance of 14-3-3 Self-Dimerization for Phosphorylation-dependent Target Binding
    • DOI 10.1091/mbc.E02-12-0821
    • Shen, Y. H., Godlewski, J., Bronisz, A., Zhu, J., Comb, M. J., Avruch, J., and Tzivion, G. (2003) Significance of 14-3-3 self-dimerization for phosphorylation- dependent target binding. Mol. Biol. Cell 14, 4721-4733 (Pubitemid 37444669)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.11 , pp. 4721-4733
    • Shen, Y.H.1    Godlewski, J.2    Bronisz, A.3    Zhu, J.4    Comb, M.J.5    Avruch, J.6    Tzivion, G.7
  • 60
    • 23744478870 scopus 로고    scopus 로고
    • Give lipids a START: The StAR-related lipid transfer (START) domain in mammals
    • DOI 10.1242/jcs.02485
    • Alpy, F., and Tomasetto, C. (2005) Give lipids a START. The StAR-related lipid transfer (START) domain in mammals. J. Cell Sci. 118, 2791-2801 (Pubitemid 41136357)
    • (2005) Journal of Cell Science , vol.118 , Issue.13 , pp. 2791-2801
    • Alpy, F.1    Tomasetto, C.2
  • 61
    • 0033180582 scopus 로고    scopus 로고
    • Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding
    • DOI 10.1016/S1097-2765(00)80363-9
    • Rittinger, K., Budman, J., Xu, J., Volinia, S., Cantley, L. C., Smerdon, S. J., Gamblin, S. J., and Yaffe, M. B. (1999) Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol. Cell 4, 153-166 (Pubitemid 29456884)
    • (1999) Molecular Cell , vol.4 , Issue.2 , pp. 153-166
    • Rittinger, K.1    Budman, J.2    Xu, J.3    Volinia, S.4    Cantley, L.C.5    Smerdon, S.J.6    Gamblin, S.J.7    Yaffe, M.B.8
  • 62
    • 0028786533 scopus 로고
    • Molecular cloning and in vivo expression of the bovine steroidogenic acute regulatory protein
    • Hartung, S., Rust, W., Balvers, M., and Ivell, R. (1995) Molecular cloning and in vivo expression of the bovine steroidogenic acute regulatory protein. Biochem. Biophys. Res. Commun. 215, 646-653
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 646-653
    • Hartung, S.1    Rust, W.2    Balvers, M.3    Ivell, R.4
  • 64
    • 0028101282 scopus 로고
    • cDNA cloning and characterization of mitochondrial import stimulation factor (MSF) purified from rat liver cytosol
    • Alam, R., Hachiya, N., Sakaguchi, M., Kawabata, S., Iwanaga, S., Kitajima, M., Mihara, K., and Omura, T. (1994) cDNA cloning and characterization of mitochondrial import stimulation factor (MSF) purified from rat liver cytosol. J. Biochem. 116, 416-425 (Pubitemid 24265619)
    • (1994) Journal of Biochemistry , vol.116 , Issue.2 , pp. 416-425
    • Alam, R.1    Hachiya, N.2    Sakaguchi, M.3    Kawabata, I.S.4    Iwanaga, S.5    Kitajima, M.6    Mihara, K.7    Omura, T.8
  • 65
    • 0027418577 scopus 로고
    • A mitochondrial import factor purified from rat liver cytosol is an ATP-dependent conformational modulator for precursor proteins
    • Hachiya, N., Alam, R., Sakasegawa, Y., Sakaguchi, M., Mihara, K., and Omura, T. (1993) A mitochondrial import factor purified from rat liver cytosol is an ATP-dependent conformational modulator for precursor proteins. EMBO J. 12, 1579-1586 (Pubitemid 23112812)
    • (1993) EMBO Journal , vol.12 , Issue.4 , pp. 1579-1586
    • Hachiya, N.1    Alam, R.2    Sakasegawa, Y.3    Sakaguchi, M.4    Mihara, K.5    Omura, T.6
  • 66
    • 0029096887 scopus 로고
    • Reconstitution of the initial steps of mitochondrial protein import
    • Hachiya, N., Mihara, K., Suda, K., Horst, M., Schatz, G., and Lithgow, T. (1995) Reconstitution of the initial steps of mitochondrial protein import. Nature 376, 705-709
    • (1995) Nature , vol.376 , pp. 705-709
    • Hachiya, N.1    Mihara, K.2    Suda, K.3    Horst, M.4    Schatz, G.5    Lithgow, T.6
  • 67
    • 12244288339 scopus 로고    scopus 로고
    • Molecular modeling and structure-based thermodynamic analysis of the StAR protein
    • DOI 10.1081/ERC-120016817
    • Mathieu, A. P., Lavigne, P., and LeHoux, J. G. (2002) Molecular modeling and structure-based thermodynamic analysis of the StAR protein. Endocr. Res. 28, 419-423 (Pubitemid 36042495)
    • (2002) Endocrine Research , vol.28 , Issue.4 , pp. 419-423
    • Mathieu, A.P.1    Lavigne, P.2    LeHoux, J.-G.3
  • 68
    • 0036918153 scopus 로고    scopus 로고
    • Insights into steroidogenic acute regulatory protein (StAR)-dependent cholesterol transfer in mitochondria: Evidence from molecular modeling and structure-based thermodynamics supporting the existence of partially unfolded states of StAR
    • DOI 10.1677/jme.0.0290327
    • Mathieu, A. P., Fleury, A., Ducharme, L., Lavigne, P., and LeHoux, J. G. (2002) Insights into steroidogenic acute regulatory protein (StAR)-dependent cholesterol transfer in mitochondria. Evidence from molecular modeling and structure-based thermodynamics supporting the existence of partially unfolded states of StAR. J. Mol. Endocrinol. 29, 327-345 (Pubitemid 36024548)
    • (2002) Journal of Molecular Endocrinology , vol.29 , Issue.3 , pp. 327-345
    • Mathieu, A.P.1    Fleury, A.2    Ducharme, L.3    Lavigne, P.4    LeHoux, J.-G.5


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