Evidence for NL1-independent nuclear translocation of the mineralocorticoid receptor
In the absence of hormone, corticosteroid receptors are primarily located in the cytoplasm, and they rapidly accumulate in the nucleus (t0.5 = 5 min) upon ligand binding. It is generally believed that the dissociation of hsp90 from the receptor is an absolute requirement for allowing its nuclear tra...
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2007
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| LEADER | 17824caa a22015377a 4500 | ||
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| 001 | PAPER-6723 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203626.0 | ||
| 008 | 190411s2007 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-33846781599 | |
| 024 | 7 | |2 cas |a aldosterone, 52-39-1, 6251-69-0; digitonin, 11024-24-1; Aldosterone, 52-39-1; HSP90 Heat-Shock Proteins; Nuclear Localization Signals; Receptors, Mineralocorticoid | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a BICHA | ||
| 100 | 1 | |a Pilipuk, G.P. | |
| 245 | 1 | 0 | |a Evidence for NL1-independent nuclear translocation of the mineralocorticoid receptor |
| 260 | |c 2007 | ||
| 270 | 1 | 0 | |m Galigniana, M.D.; Fundación Instituto Leloir, Av. Patricias Argentinas 435, Buenos Aires C1405BWE, Argentina; email: mgali@leloir.org.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 504 | |a Galigniana, M.D., Radanyi, C., Renoir, J.M., Housley, P.R., Pratt, W.B., Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus (2001) J. Biol. Chem, 276, pp. 14884-14889 | ||
| 504 | |a Galigniana, M.D., Piwien Pilipuk, G., Kanelakis, K.C., Burton, G., Lantos, C.P., Molecular mechanism of activation and nuclear translocation of the mineralocorticoid receptor upon binding of pregnanesteroids (2004) Mol. Cell. Endocrinol, 217, pp. 167-179 | ||
| 504 | |a Pratt, W.B., Galigniana, M.D., Harrell, J.M., DeFranco, D.B., Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement (2004) Cell. Signalling, 16, pp. 857-872 | ||
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| 504 | |a Harrell, J.M., Kurek, I., Breiman, A., Radanyi, C., Renoir, J.M., Pratt, W.B., Galigniana, M.D., All of the protein interactions that link steroid receptor·hsp90·immunophilin heterocomplexes to cytoplasmic dynein are common to plant and animal cells (2002) Biochemistry, 41, pp. 5581-5587 | ||
| 504 | |a Wochnik, G.M., Ruegg, J., Abel, G.A., Schmidt, U., Holsboer, F., Rein, T., FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells (2005) J. Biol. Chem, 280, pp. 4609-4616 | ||
| 504 | |a Galigniana, M.D., Scruggs, J.L., Herrington, J., Welsh, M.J., Carter-Su, C., Housley, P.R., Pratt, W.B., Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton (1998) Mol. Endocrinol, 12, pp. 1903-1913 | ||
| 504 | |a Galigniana, M.D., Harrell, J.M., Housley, P.R., Patterson, C., Fisher, S.K., Pratt, W.B., Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation (2004) Brain Res. Mol. Brain Res, 123, pp. 27-36 | ||
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| 504 | |a Galigniana, M.D., Housley, P.R., DeFranco, D.B., Pratt, W.B., Inhibition of glucocorticoid receptor nucleocytoplasmic shuttling by okadaic acid requires intact cytoskeleton (1999) J. Biol. Chem, 274, pp. 16222-16227 | ||
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| 504 | |a Walther, R.F., Atlas, E., Carrigan, A., Rouleau, Y., Edgecombe, A., Visentin, L., Lamprecht, C., Lefebvre, Y.A., A serine/threonine-rich motif is one of three nuclear localization signals that determine unidirectional transport of the mineralocorticoid receptor to the nucleus (2005) J. Biol. Chem, 280, pp. 17549-17561 | ||
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| 504 | |a Piwien-Pilipuk, G., Kanelakis, K.C., Ghini, A.A., Lantos, C.P., Litwack, G., Burton, G., Galigniana, M.D., Modification of an essential amino group in the mineralocorticoid receptor evidences a differential conformational change of the receptor protein upon binding of antagonists, natural agonists and the synthetic agonist 11,19-oxidoprogesterone (2002) Biochim. Biophys. Acta, 1539, pp. 31-48 | ||
| 504 | |a Piwien-Pilipuk, G., Galigniana, M.D., Oxidative stress induced by L-buthionine-(S,R)-sulfoximine, a selective inhibitor of glutathione metabolism, abrogates mouse kidney mineralocorticoid receptor function (2000) Biochim. Biophys. Acta, 1495, pp. 263-280 | ||
| 504 | |a Piwien-Pilipuk, G., Ayala, A., Machado, A., Galigniana, M.D., Impairment of mineralocorticoid receptor (MR)-dependent biological response by oxidative stress and aging: Correlation with post-translational modification of MR and decreased ADP-ribosylatable level of elongating factor 2 in kidney cells (2002) J. Biol. Chem, 277, pp. 11896-11903 | ||
| 504 | |a Baird, F.E., Pinilla-Tenas, J.J., Ogilvie, W.L., Ganapathy, V., Hundal, H.S., Taylor, P.M., Evidence for allosteric regulation of pH-sensitive System A (SNAT2) and System N (SNAT5) amino acid transporter activity involving a conserved histidine residue (2006) Biochem. J, 397, pp. 369-375 | ||
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| 504 | |a Paraguison, R.C., Higaki, K., Sakamoto, Y., Hashimoto, O., Miyake, N., Matsumoto, H., Yamamoto, K., Nanba, E., Polyhistidine tract expansions in HOXA1 result in intranuclear aggregation and increased cell death (2005) Biochem. Biophys. Res. Commun, 336, pp. 1033-1039 | ||
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| 520 | 3 | |a In the absence of hormone, corticosteroid receptors are primarily located in the cytoplasm, and they rapidly accumulate in the nucleus (t0.5 = 5 min) upon ligand binding. It is generally believed that the dissociation of hsp90 from the receptor is an absolute requirement for allowing its nuclear translocation. However, recent evidence suggests that hsp90 may remain associated with the glucocorticoid receptor during this process, and thus, the receptor nuclear localization signal (NLS) is not obscured by its presence. To determine the requirements for mineralocorticoid receptor (MR) nuclear transport, it was first shown that in rat kidney collecting duct cells, nuclear localization of MR in the presence of aldosterone was complete in 10 min. Although the hsp90 inhibitor radicicol delayed nuclear translocation, it did not prevent complete nuclear accumulation of MR at longer incubation times (t 0.5 = 30-40 min). MR carbamylation generates a non-steroid- transformed receptor that, in contrast to native MR, is very stable in cell-free systems. In contrast to the full nuclear translocation of aldosterone- transformed MR, only a fraction of the carbamylated MR became nuclear in digitonin-permeabilized cells even though its NLS is exposed. Furthermore, while preincubation of permeabilized cells with NL1 peptide or anti-NL1 antibody fully inhibited the nuclear translocation of NL1-tagged albumin, neither treatment fully inhibited MR nuclear translocation. We postulate that there are at least two possible mechanisms for MR nuclear translocation. One of them is hsp90- and NL1-dependent, and the other functions in a manner that is independent of the classical pathway. © 2007 American Chemical Society. |l eng | |
| 593 | |a Fundación Instituto Leloir, Av. Patricias Argentinas 435, Buenos Aires C1405BWE, Argentina | ||
| 593 | |a Fundación Instituto Leloir, CONICET, Buenos Aires, Argentina | ||
| 593 | |a School of Biological Sciences, Queen Mary, University of London, London, United Kingdom | ||
| 593 | |a Division of Endocrinology, University of Mississippi Medical Center, Jackson, MS 39216, United States | ||
| 593 | |a Departamento de Química Biológica, Facultad de Ciencias Exactas Y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a ANTIBODIES |
| 690 | 1 | 0 | |a BIOLOGICAL ORGANS |
| 690 | 1 | 0 | |a CELLS |
| 690 | 1 | 0 | |a CHEMICAL BONDS |
| 690 | 1 | 0 | |a DISSOCIATION |
| 690 | 1 | 0 | |a HORMONES |
| 690 | 1 | 0 | |a PROTEINS |
| 690 | 1 | 0 | |a GLUCOCORTICOID RECEPTORS |
| 690 | 1 | 0 | |a MINERALOCORTICOID RECEPTOR (MR) |
| 690 | 1 | 0 | |a NUCLEAR ACCUMULATION |
| 690 | 1 | 0 | |a NUCLEAR LOCALIZATION SIGNALS (NLS) |
| 690 | 1 | 0 | |a NEUROLOGY |
| 690 | 1 | 0 | |a ALDOSTERONE |
| 690 | 1 | 0 | |a CORTICOSTEROID RECEPTOR |
| 690 | 1 | 0 | |a DIGITONIN |
| 690 | 1 | 0 | |a HEAT SHOCK PROTEIN 90 |
| 690 | 1 | 0 | |a MINERALOCORTICOID RECEPTOR |
| 690 | 1 | 0 | |a ANIMAL CELL |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CARBAMOYLATION |
| 690 | 1 | 0 | |a CELL MEMBRANE PERMEABILITY |
| 690 | 1 | 0 | |a CELL NUCLEUS |
| 690 | 1 | 0 | |a CONTROLLED STUDY |
| 690 | 1 | 0 | |a CYTOPLASM |
| 690 | 1 | 0 | |a DISSOCIATION |
| 690 | 1 | 0 | |a KIDNEY COLLECTING TUBULE |
| 690 | 1 | 0 | |a LIGAND BINDING |
| 690 | 1 | 0 | |a MOUSE |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a NUCLEAR LOCALIZATION SIGNAL |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN LOCALIZATION |
| 690 | 1 | 0 | |a RAT |
| 690 | 1 | 0 | |a ACTIVE TRANSPORT, CELL NUCLEUS |
| 690 | 1 | 0 | |a ALDOSTERONE |
| 690 | 1 | 0 | |a ANIMALS |
| 690 | 1 | 0 | |a HSP90 HEAT-SHOCK PROTEINS |
| 690 | 1 | 0 | |a KIDNEY |
| 690 | 1 | 0 | |a KINETICS |
| 690 | 1 | 0 | |a NUCLEAR LOCALIZATION SIGNALS |
| 690 | 1 | 0 | |a RATS |
| 690 | 1 | 0 | |a RECEPTORS, MINERALOCORTICOID |
| 690 | 1 | 0 | |a RATTUS |
| 700 | 1 | |a Vinson, G.P. | |
| 700 | 1 | |a Sanchez, C.G. | |
| 700 | 1 | |a Galigniana, M.D. | |
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