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Chicken thyroid hormone receptor α requires the N‐terminal amino acids for exclusive nuclear localization
Author(s) -
Andersson Monika L,
Vennström Björn
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01223-4
Subject(s) - subcellular localization , thyroid hormone receptor alpha , nuclear localization sequence , serine , thyroid hormone receptor , cytoplasm , amino acid , receptor , thyroid , nuclear receptor , alpha (finance) , nuclear export signal , hormone , nucleus , chemistry , phosphorylation , cell nucleus , biology , microbiology and biotechnology , endocrinology , biochemistry , gene , medicine , transcription factor , nursing , patient satisfaction , construct validity
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.