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J Mol Biochem. 2017;6(1):3-12. Epub 2017 Apr 15.

The Role of S-Palmitoylation of the Human Glucocorticoid Receptor (hGR) in Mediating the Nongenomic Glucocorticoid Actions.

Author information

1
Division of Endocrinology and Metabolism, Center of Clinical, Experimental Surgery and Translational Research, Biomedical Research Foundation of the Academy of Athens, Athens, Greece.
2
Division of Endocrinology, Metabolism and Diabetes, First Department of Pediatrics, National and Kapodistrian University of Athens Medical School, "Aghia Sophia" Children's Hospital, Athens, Greece.
3
Program in Reproductive and Adult Endocrinology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland.
4
Division of Hematology-Oncology, Basic Research Center, Biomedical Research Foundation of the Academy of Athens, Athens, Greece.
5
Department of Clinical Biochemistry, University of Athens Medical School, "Attiko" Hospital, Athens, 12462, Greece.
6
Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, 41221, Greece.
7
Saudi Diabetes Study Research Group, King Fahd Center for Medical Research, King Abdulaziz University, Jeddah, Saudi Arabia.

Abstract

BACKGROUND:

Many rapid nongenomic glucocorticoid actions are mediated by membrane-bound glucocorticoid receptors (GRs). S-palmitoylation is a lipid post-translational modification that mediates the membrane localization of some steroid receptors. A highly homologous amino acid sequence (663YLCM KTLLL671) is present in the ligand-binding domain of hGRα, suggesting that hGRα might also undergo S-palmitoylation.

AIM:

To investigate the role of the motif 663YLCMKTLLL671 in membrane localization of the hGRα and in mediating rapid nongenomic glucocorticoid signaling.

METHODS AND RESULTS:

We showed that the mutant receptors hGRαY663A, hGRαC665A and hGRαLL670/671AA, and the addition of the palmitoylation inhibitor 2-bromopalmitate did not prevent membrane localization of hGRα and co-localization with caveolin-1, and did not influence the biphasic activation of mitogen-activated protein kinase (MAPK) signaling pathway in the early time points. Finally, the hGRα was not shown to undergo S-palmitoylation.

CONCLUSIONS:

The motif 663YLCMKTLLL671 does not play a role in membrane localization of hGRα and does not mediate the nongenomic glucocorticoid actions.

PMID:
28775968
PMCID:
PMC5538142

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