Chicken thyroid hormone receptor α requires the N‐terminal amino acids for exclusive nuclear localization
- 27 October 1997
- journal article
- Published by Wiley in FEBS Letters
- Vol. 416 (3) , 291-296
- https://doi.org/10.1016/s0014-5793(97)01223-4
Abstract
The subcellular localization of natural and engineered forms of the chicken thyroid hormone receptor (cTRα) is dependent on amino acids encoded in the N‐terminal region. The full length receptor protein, cTRα‐p46, was found to localize exclusively to the nucleus, whereas the N‐terminally shorter variant, cTRα‐p40, localizes to both the nucleus and the cytoplasm. The exclusive nuclear localization of cTRα‐p46 is dependent on the presence of the first 11 N‐terminal amino acids, but independent of the phosphorylation of the serine at position 12. Our data identify a novel role for an N‐terminal domain of the full length thyroid hormone receptor.Keywords
This publication has 43 references indexed in Scilit:
- The nuclear receptor superfamily: The second decadeCell, 1995
- Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporinsCell, 1995
- Transcriptional activation: A complex puzzle with few easy piecesCell, 1994
- The nuclear pore complex and nucleocytoplasmic transportCurrent Opinion in Cell Biology, 1993
- Cross-Linking of Estrogen Receptor to Chromatin in Intact MCF-7 Human Breast Cancer Cells: Optimization and Effect of LigandMolecular Endocrinology, 1990
- Steroid Receptor Family: Structure and FunctionsEndocrine Reviews, 1990
- Signal transduction by steroid hormones: nuclear localization is differentially regulated in estrogen and glucocorticoid receptors.Cell Regulation, 1990
- A movable and regulable inactivation function within the steroid binding domain of the glucocorticoid receptorCell, 1988
- The Steroid and Thyroid Hormone Receptor SuperfamilyScience, 1988
- A short amino acid sequence able to specify nuclear locationCell, 1984