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J Steroid Biochem Mol Biol. 1998 Apr;65(1-6):51-8.

Molecular chaperones and subcellular trafficking of steroid receptors.

Author information

1
Department of Biological Sciences, University of Pittsburgh, PA 15260, USA. dod1@vms.cis.pitt.edu

Abstract

Unliganded steroid receptors exist as heteromeric complexes comprised of heat shock and immunophilin proteins that associate either directly or indirectly with receptor carboxyl-terminal ligand-binding domains. Molecular chaperons, and other proteins associated with steroid receptors, play an important role in the maturation of receptors to a hormone-binding competent state. Steroid receptor-associated 90 and 70 kDa heat shock proteins, hsp90 and hsp70, respectively, have well established roles in protein folding in addition to participating in numerous subcellular trafficking pathways. In this review, we discuss the possible roles that molecular chaperons, such as hsp90, hsp70 and DnaJ proteins, have in steroid receptor trafficking within two distinct subcellular compartments, i.e. the cytoplasm and nucleus.

PMID:
9699857
DOI:
10.1016/s0960-0760(97)00177-5
[Indexed for MEDLINE]

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