RGD Reference Report - Regulation of thyroid hormone receptor alpha2 RNA binding and subcellular localization by phosphorylation. - Rat Genome Database

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Regulation of thyroid hormone receptor alpha2 RNA binding and subcellular localization by phosphorylation.

Authors: Xu, B  Koenig, RJ 
Citation: Xu B and Koenig RJ, Mol Cell Endocrinol. 2005 Dec 21;245(1-2):147-57. Epub 2005 Dec 13.
RGD ID: 1580096
Pubmed: PMID:16356627   (View Abstract at PubMed)
DOI: DOI:10.1016/j.mce.2005.11.010   (Journal Full-text)

Thyroid hormone receptor alpha2 (TRalpha2) is an alternative splice product of the TRalpha primary transcript whose unique carboxyl terminus does not bind T3 or activate transcription. The physiological function of TRalpha2 is unknown. We have found that TRalpha2 is a single stranded RNA binding protein and that the RNA binding domain localizes to a 41 amino acid region immediately distal to the second zinc finger. TRalpha2 contains a single protein kinase CK2 phosphorylation site in its amino terminus and potentially nine CK2 sites in its unique carboxyl terminus. In vitro CK2 treatment of TRalpha2 eliminated its RNA binding. Mutational analysis indicated that phosphorylations at the N- and C-terminal sites both contribute to this inhibitory effect. Cellular localization studies demonstrated that phosphorylated TRalpha2 is primarily cytoplasmic, whereas unphosphorylated TRalpha2 is primarily nuclear. Since RNA binding is a property of unphosphorylated TRalpha2, the TRalpha2-RNA interaction likely represents a nuclear function of TRalpha2.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
single-stranded RNA binding  IDA 1580096; 1580096 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Thra  (thyroid hormone receptor alpha)
Thra_v2  (thyroid hormone receptor alpha, variant 2)

Objects referenced in this article
Gene Thra_v1 thyroid hormone receptor alpha, variant 1 Rattus norvegicus

Additional Information