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Human Spot 14 protein interacts physically and functionally with the thyroid receptor
Author(s) -
Huang ShihMing,
Cheng YiShan,
Liu ShuTing,
Liu PeiYao
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a253-c
Subject(s) - receptor , biology , gene , gene expression , thyroid , carcinogenesis , thyroid hormone receptor beta , nuclear receptor , thyroid hormone receptor , aryl hydrocarbon receptor nuclear translocator , microbiology and biotechnology , biochemistry , transcription factor , genetics , aryl hydrocarbon receptor , cancer , hormone receptor , breast cancer
Spot 14 (S14) is a small acidic protein with no sequence similarity to other mammalian gene products. Its biochemical function is elusive. Recent studies have shown that, in some cancers, human S14 (hS14) localizes to the nucleus and is amplified, suggesting that it plays a role in the regulation of lipogenic enzymes during tumorigenesis. In this study, we purified untagged hS14 protein and then demonstrated, using various biochemical methods, including analytic ultracentrifugation, that hS14 might form a homodimer. We also found several lines of evidence to suggest physical and functional interactions between hS14 and the thyroid receptor. The ubiquitous expression of hS14 in various cell lines and its cell‐type‐dependent functions demonstrated in this study suggest that it acts as a positive or negative cofactor of the thyroid receptor to regulate malate dehydrogenase gene expression. These findings provide a molecular rationale for the role of hS14 in thyroid‐receptor‐dependent transcriptional activation of the expression of specific genes.