Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Sci. STKE, 25 June 2002
Vol. 2002, Issue 138, p. re9
[DOI: 10.1126/stke.2002.138.re9]

REVIEWS

Rapid Actions of Steroid Receptors in Cellular Signaling Pathways

Andrew C. B. Cato1*, Andrea Nestl1, and Sigrun Mink2

1Forschungszentrum Karlsruhe, Institute of Toxicology and Genetics, Post Office Box 3640, D-76021 Karlsruhe, Germany.
2G2M Cancer Drugs AG South, Forschungszentrum Karlsruhe, Hermann-von-Helmholtz-Platz 1, D-76344 Eggenstein-Leopoldshafen, Germany.

Abstract: Steroid hormones regulate cellular processes by binding to intracellular receptors that, in turn, interact with discrete nucleotide sequences to alter gene expression. Because most steroid receptors in target cells are located in the cytoplasm, they need to get into the nucleus to alter gene expression. This process typically takes at least 30 to 60 minutes. In contrast, other regulatory actions of steroid hormones are manifested within seconds to a few minutes. These time periods are far too rapid to be due to changes at the genomic level and are therefore termed nongenomic or rapid actions, to distinguish them from the classical steroid hormone action of regulation of gene expression. The rapid effects of steroid hormones are manifold, ranging from activation of mitogen-activated protein kinases (MAPKs), adenylyl cyclase (AC), protein kinase C (PKC), and heterotrimeric guanosine triphosphate-binding proteins (G proteins). In some cases, these rapid actions of steroids are mediated through the classical steroid receptor that can also function as a ligand-activated transcription factor, whereas in other instances the evidence suggests that these rapid actions do not involve the classical steroid receptors. One candidate target for the nonclassical receptor-mediated effects are G protein-coupled receptors (GPCRs), which activate several signal transduction pathways. One characteristic of responses that are not mediated by the classical steroid receptors is insensitivity to steroid antagonists, which has contributed to the notion that a new class of steroid receptors may be responsible for part of the rapid action of steroids. Evidence suggests that the classical steroid receptors can be localized at the plasma membrane, where they may trigger a chain of reactions previously attributed only to growth factors. Identification of interaction domains on the classical steroid receptors involved in the rapid effects, and separation of this function from the genomic action of these receptors, should pave the way to a better understanding of the rapid action of steroid hormones.

*Corresponding author. Telephone, +49 7247 822146; fax, +49 7242 823354; e-mail, andrew.cato{at}igen.fzk.de

Citation: A. C. B. Cato, A. Nestl, S. Mink, Rapid Actions of Steroid Receptors in Cellular Signaling Pathways. Sci. STKE 2002, re9 (2002).

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
SHON Is a Novel Estrogen-Regulated Oncogene in Mammary Carcinoma That Predicts Patient Response to Endocrine Therapy.
Y. Jung, T. M. A. Abdel-Fatah, S. Y. T. Chan, C. C. Nolan, A. R. Green, I. O. Ellis, L. Li, B. Huang, J. Lu, B. Xu, et al. (2013)
Cancer Res. 73, 6951-6962
   Abstract »    Full Text »    PDF »
Membrane Glucocorticoid Receptor Activation Induces Proteomic Changes Aligning with Classical Glucocorticoid Effects.
S. Vernocchi, N. Battello, S. Schmitz, D. Revets, A. M. Billing, J. D. Turner, and C. P. Muller (2013)
Mol. Cell. Proteomics 12, 1764-1779
   Abstract »    Full Text »    PDF »
Sperm metabolism in pigs: a role for peroxisome proliferator-activated receptor gamma (PPAR{gamma}).
M. Santoro, C. Guido, F. De Amicis, D. Sisci, D. Vizza, S. Gervasi, A. Carpino, and S. Aquila (2013)
J. Exp. Biol. 216, 1085-1092
   Abstract »    Full Text »    PDF »
Nongenomic glucocorticoid receptor action regulates gap junction intercellular communication and neural progenitor cell proliferation.
R. A. Samarasinghe, R. Di Maio, D. Volonte, F. Galbiati, M. Lewis, G. Romero, and D. B. DeFranco (2011)
PNAS 108, 16657-16662
   Abstract »    Full Text »    PDF »
Glucocorticoid regulation of human pulmonary surfactant protein-B (SP-B) mRNA stability is independent of activated glucocorticoid receptor.
C. C. Tillis, H. W. Huang, W. Bi, S. Pan, S. R. Bruce, and J. L. Alcorn (2011)
Am J Physiol Lung Cell Mol Physiol 300, L940-L950
   Abstract »    Full Text »    PDF »
GPRC6A Mediates the Non-genomic Effects of Steroids.
M. Pi, A. L. Parrill, and L. D. Quarles (2010)
J. Biol. Chem. 285, 39953-39964
   Abstract »    Full Text »    PDF »
Differential Protein Expression Profiles in Estrogen Receptor-Positive and -Negative Breast Cancer Tissues Using Label-Free Quantitative Proteomics.
K. Rezaul, J. K. Thumar, D. H. Lundgren, J. K. Eng, K. P. Claffey, L. Wilson, and D. K. Han (2010)
Genes & Cancer 1, 251-271
   Abstract »    Full Text »    PDF »
SIGNAL TRANSDUCTION: A New Mediator for an Old Hormone?.
S. C. Hewitt, B. J. Deroo, and K. S. Korach (2005)
Science 307, 1572-1573
   Abstract »    Full Text »    PDF »

To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882