Regulation of steroid receptor subcellular trafficking

被引:41
作者
DeFranco D.B. [1 ]
机构
[1] Department of Biological Sciences, University of Pittsburgh, Pittsburgh
关键词
Glucocorticoid receptor; nuclear import; nuclear export; nucleocytoplasmic shuttling; nuclear matrix; heat shock proteins;
D O I
10.1007/BF02737882
中图分类号
学科分类号
摘要
Cellular responses to external signals often reflect alterations in gene expression. The activation of cell surface hormone or growth factor receptors upon the binding of appropriate ligands mobilizes signal transduction cascades that can ultimately impact the activity of defined sets of transcription factors. The interpretation of hormonal signals can also be initiated intracellularly, as is the case for steroid hormone receptors. In addition to recognizing specific hormones, steroid hormone receptors also function as transcription factors and directly transduce hormonal signals to activation or repression of unique target genes. The delivery of activated steroid receptors to high-affinity genomic sites must be efficient to account for the rapidity and selectivity of many transcriptional responses to steroid hormones. Thus, the signal transduction capacity of steroid hormone receptors will be affected by the efficiency of receptor trafficking both between different subcellular compartments (i.e., the cytoplasm and nucleus) and within a specific compartment (i.e., the nucleus). This article will highlight the recent advances in our understanding of subcellular and subnuclear trafficking of steroid receptors.
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页码:1 / 24
页数:23
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共 96 条
[71]  
Dworetzky, S.I., Wright, K.L., Fey, E.G., Penman, S., Lian, J.B., Stein, J.L., Stein, G.S., Sequence-specific DNA binding proteins are components of a nuclear matrix attachment site (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 4178-4182
[72]  
Gasser, S.M., Laemmli, U.K., Cohabitation of scaffold binding regions with upstream/enhancer elements of three developmentally regulated Drosophila melanogaster genes (1986) Cell, 46, pp. 521-530
[73]  
Georgopoulos, C., Welch, W.J., Role of the major heat shock proteins as molecular chaperones (1993) Ann. Rev. Cell Biol., 9, pp. 601-634
[74]  
Hendrick, J.P., Hartl, F.-U., Molecular chaperone functions of heat-shock proteins (1993) Ann. Rev. Biochem., 62, pp. 349-384
[75]  
Csermely, P., Schnaider, T., Szanto, I., Signalling and transport through the nuclear membrane (1995) Biochim. Biophys. Acta, 1241, pp. 425-452
[76]  
Gasc, J.-M., Renoir, J.-M., Delahaye, F., Baulieu, E.-E., Nuclear localization of two steroid receptor-associated proteins, hsp90 and p59 (1990) Exp. Cell Res., 186, pp. 362-367
[77]  
Mandell, R.B., Feldherr, C.M., Identification of two HSP70-related Xenopus oocyte proteins that are capable of recycling across the nuclear envelope (1990) J. Cell Biol., 111, pp. 1775-1783
[78]  
Lewis, M.J., Pelham, H.R.B., Involvement of ATP in the nuclear and nucleolar functions of the 70 kd heat shock protein (1985) EMBO J., 4, pp. 3137-3143
[79]  
Liu, Y., Liang, S., Tartakoff, A.M., Heat shock disassembles the nucleolus and inhibits nuclear protein import and poly(A)+ RNA export (1996) EMBO J., 15, pp. 6750-6757
[80]  
Shaknovich, R., Shue, G., Kohtz, S., Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84) (1992) Mol. Cell. Biol., 12, pp. 5059-5068