메뉴 건너뛰기




Volumn 295, Issue 1, 2008, Pages

Proteins interact with the cytosolic mineralocorticoid receptor depending on the ligand

Author keywords

Aldosterone; Mineralocorticoid; Proteomics; Spironolactone; 14 3 3; Steroid receptor

Indexed keywords

MINERALOCORTICOID RECEPTOR; PROPIONYL COENZYME A; SPIRONOLACTONE; STEROID RECEPTOR; ALDOSTERONE; ALDOSTERONE ANTAGONIST; CHAPERONE; HEAT SHOCK PROTEIN; HYBRID PROTEIN; LIGAND; METHYLMALONYL COENZYME A DECARBOXYLASE; MOLECULAR CHAPERONE GRP78; PROTEIN 14 3 3; SIGNAL PEPTIDE; YWHAE PROTEIN, HUMAN;

EID: 49849102946     PISSN: 03636135     EISSN: 15221539     Source Type: Journal    
DOI: 10.1152/ajpheart.00825.2007     Document Type: Article
Times cited : (10)

References (22)
  • 2
    • 0024567048 scopus 로고
    • Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor
    • Bresnick EH, Dalman FC, Sanchez ER, Pratt WB. Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor. J Biol Chem 264: 4992-4997, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 4992-4997
    • Bresnick, E.H.1    Dalman, F.C.2    Sanchez, E.R.3    Pratt, W.B.4
  • 3
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen C, Okayama H. High-efficiency transformation of mammalian cells by plasmid DNA. Mol Cell Biol 7: 2745-2752, 1987.
    • (1987) Mol Cell Biol , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 4
    • 0016440506 scopus 로고
    • On the association of glycolytic enzymes with structural proteins of skeletal muscle
    • Clarke FM, Masters CJ. On the association of glycolytic enzymes with structural proteins of skeletal muscle. Biochim Biophys Acta 381: 37-46, 1975.
    • (1975) Biochim Biophys Acta , vol.381 , pp. 37-46
    • Clarke, F.M.1    Masters, C.J.2
  • 5
    • 0027743317 scopus 로고
    • Heat shock protein 70 is associated in substoichiometric amounts with the rat hepatic glucocorticoid receptor
    • Diehl EE, Schmidt TJ. Heat shock protein 70 is associated in substoichiometric amounts with the rat hepatic glucocorticoid receptor. Biochemistry 32: 13510-13515, 1993.
    • (1993) Biochemistry , vol.32 , pp. 13510-13515
    • Diehl, E.E.1    Schmidt, T.J.2
  • 8
    • 0029867062 scopus 로고    scopus 로고
    • Human mineralocorticoid receptor interacts with actin under mineralocorticoid ligand modulation
    • Jalaguier S, Mornet D, Mesnier D, Leger JJ, Auzou G. Human mineralocorticoid receptor interacts with actin under mineralocorticoid ligand modulation. FEBS Lett 384: 112-116, 1996.
    • (1996) FEBS Lett , vol.384 , pp. 112-116
    • Jalaguier, S.1    Mornet, D.2    Mesnier, D.3    Leger, J.J.4    Auzou, G.5
  • 9
    • 0028027504 scopus 로고
    • A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23
    • Johnson JL, Toft DO. A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23. J Biol Chem 269: 24989-24993, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 24989-24993
    • Johnson, J.L.1    Toft, D.O.2
  • 10
    • 0038152840 scopus 로고    scopus 로고
    • Protein 14-3-3sigma interacts with and favors cytoplasmic subcellular localization of the glucocorticoid receptor, acting as a negative regulator of the glucocorticoid signaling pathway
    • Kino T, Souvatzoglou E, De Martino MU, Tsopanomihalu M, Wan Y, Chrousos GP. Protein 14-3-3sigma interacts with and favors cytoplasmic subcellular localization of the glucocorticoid receptor, acting as a negative regulator of the glucocorticoid signaling pathway. J Biol Chem 278: 25651-25656, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 25651-25656
    • Kino, T.1    Souvatzoglou, E.2    De Martino, M.U.3    Tsopanomihalu, M.4    Wan, Y.5    Chrousos, G.P.6
  • 12
    • 0029022285 scopus 로고
    • Prerequisite for cardiac aldosterone action. Mineralocorticoid receptor and 11 beta-hydroxysteroid dehydrogenase in the human heart
    • Lombes M, Alfaidy N, Eugene E, Lessana A, Farman N, Bonvalet JP. Prerequisite for cardiac aldosterone action. Mineralocorticoid receptor and 11 beta-hydroxysteroid dehydrogenase in the human heart. Circulation 92: 175-182, 1995.
    • (1995) Circulation , vol.92 , pp. 175-182
    • Lombes, M.1    Alfaidy, N.2    Eugene, E.3    Lessana, A.4    Farman, N.5    Bonvalet, J.P.6
  • 13
    • 33750489051 scopus 로고    scopus 로고
    • An inherent role of microtubule network in the action of nuclear receptor
    • Manavathi B, Acconcia F, Rayala SK, Kumar R. An inherent role of microtubule network in the action of nuclear receptor. Proc Natl Acad Sci USA 103: 15981-15986, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15981-15986
    • Manavathi, B.1    Acconcia, F.2    Rayala, S.K.3    Kumar, R.4
  • 14
    • 0037205403 scopus 로고    scopus 로고
    • Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation
    • Misra P, Qi C, Yu S, Shah SH, Cao WQ, Rao MS, Thimmapaya B, Zhu Y, Reddy JK. Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation. J Biol Chem 277: 20011-20019, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 20011-20019
    • Misra, P.1    Qi, C.2    Yu, S.3    Shah, S.H.4    Cao, W.Q.5    Rao, M.S.6    Thimmapaya, B.7    Zhu, Y.8    Reddy, J.K.9
  • 15
    • 17844395675 scopus 로고    scopus 로고
    • The elongation factor ELL (eleven-nineteen lysine-rich leukemia) is a selective coregulator for steroid receptor functions
    • Pascual-Le Tallec L, Simone F, Viengchareun S, Meduri G, Thirman MJ, Lombes M. The elongation factor ELL (eleven-nineteen lysine-rich leukemia) is a selective coregulator for steroid receptor functions. Mol Endocrinol 19: 1158-1169, 2005.
    • (2005) Mol Endocrinol , vol.19 , pp. 1158-1169
    • Pascual-Le Tallec, L.1    Simone, F.2    Viengchareun, S.3    Meduri, G.4    Thirman, M.J.5    Lombes, M.6
  • 16
    • 2342651419 scopus 로고    scopus 로고
    • 14-3-3-Affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking
    • Pozuelo Rubio M, Geraghty KM, Wong BH, Wood NT, Campbell DG, Morrice N, Mackintosh C. 14-3-3-Affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking. Biochem J 379: 395-408, 2004.
    • (2004) Biochem J , vol.379 , pp. 395-408
    • Pozuelo Rubio, M.1    Geraghty, K.M.2    Wong, B.H.3    Wood, N.T.4    Campbell, D.G.5    Morrice, N.6    Mackintosh, C.7
  • 18
    • 0027214981 scopus 로고
    • Glycolytic enzymes as DNA binding proteins
    • Ronai Z. Glycolytic enzymes as DNA binding proteins. Int J Biochem 25: 1073-1076, 1993.
    • (1993) Int J Biochem , vol.25 , pp. 1073-1076
    • Ronai, Z.1
  • 19
    • 0026570948 scopus 로고
    • Immunolocalization of mineralocorticoid receptor in human kidney, pancreas, salivary, mammary and sweat glands: A light and electron microscopic immunohistochemical study
    • Sasano H, Fukushima K, Sasaki I, Matsuno S, Nagura H, Krozowski ZS. Immunolocalization of mineralocorticoid receptor in human kidney, pancreas, salivary, mammary and sweat glands: a light and electron microscopic immunohistochemical study. J Endocrinol 132: 305-310, 1992.
    • (1992) J Endocrinol , vol.132 , pp. 305-310
    • Sasano, H.1    Fukushima, K.2    Sasaki, I.3    Matsuno, S.4    Nagura, H.5    Krozowski, Z.S.6
  • 20
    • 0037192501 scopus 로고    scopus 로고
    • Molecular determinants for the tissue specificity of SERMs
    • Shang Y, Brown M. Molecular determinants for the tissue specificity of SERMs. Science 295: 2465-2468, 2002.
    • (2002) Science , vol.295 , pp. 2465-2468
    • Shang, Y.1    Brown, M.2
  • 21
    • 0030887128 scopus 로고    scopus 로고
    • Interaction of the ligand-activated glucocorticoid receptor with the 14-3-3 eta protein
    • Wakui H, Wright AP, Gustafsson J, Zilliacus J. Interaction of the ligand-activated glucocorticoid receptor with the 14-3-3 eta protein. J Biol Chem 272: 8153-8156, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 8153-8156
    • Wakui, H.1    Wright, A.P.2    Gustafsson, J.3    Zilliacus, J.4
  • 22
    • 0035964208 scopus 로고    scopus 로고
    • Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function
    • Zhu Y, Qi C, Cao WQ, Yeldandi AV, Rao MS, Reddy JK. Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function. Proc Natl Acad Sci USA 98: 10380-10385, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10380-10385
    • Zhu, Y.1    Qi, C.2    Cao, W.Q.3    Yeldandi, A.V.4    Rao, M.S.5    Reddy, J.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.