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Mutations in squirrel monkey glucocorticoid receptor impair nuclear translocation JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY Her, S., Patel, P. D., Schatzberg, A. F., Lyons, D. M. 2005; 94 (4): 319-326

Abstract

To identify the determinants of impaired glucocorticoid receptor (GR) signaling in a model of glucocorticoid resistance, cloned GR from Guyanese squirrel monkeys (gsmGR) was tagged with enhanced green fluorescent protein, and nuclear translocation was examined in transfected COS1 cells. In keeping with evidence that gsmGR transactivational competence is impaired, we found that nuclear translocation is likewise diminished in gsmGR relative to human GR (hGR). Experiments with GR chimeras revealed that replacement of the gsmGR ligand binding domain (LBD) with that from hGR increased translocation. Truncated gsmGR constructs lacking the LDB after amino acid 552 also showed increased translocation even in the absence of cortisol. Three back-mutations of gsmGR to hGR (Thr551Ser, Ala616Ser, and Ser618Ala) in the LBD confirmed that these amino acids play a role in diminished translocation.

View details for DOI 10.1016/j.jsbmb.2004.11.010

View details for Web of Science ID 000229445800005

View details for PubMedID 15857751