The delivery of activated steroid receptors to high-affinity genomic sites must be efficient enough 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 influenced by the efficiency of receptor trafficking both between different subcellular compartments (that is, the cytoplasm and nucleus) and within a specific compartment (that is, the nucleus). Molecular chaperones, such as heat shock proteins, have long been recognized to play important roles in the management of protein folding in both stressed and nonstressed cells. In recent years, the participation of these proteins in various signal transduction pathways (for example, steroid hormone responses) has also been recognized. In this review, recent results that implicate a role for distinct heat shock proteins in subnuclear trafficking of glucocorticoid receptors are discussed. These studies also highlight the importance of mobilizing the cellular chaperone machinery for managing steroid receptor folding within the nucleus.