A zinc finger HIT domain-containing protein, ZNHIT-1, interacts with orphan nuclear hormone receptor Rev-erbβ and removes Rev-erbβ-induced inhibition of apoCIII transcription

16Citations
Citations of this article
12Readers
Mendeley users who have this article in their library.

Abstract

The orphan receptors, Rev-erbα and Rev-erbβ, are members of the nuclear receptor superfamily and specifically repress apolipoprotein CIII (apoCIII) gene expression in rats and humans. Moreover, Rev-erbα null mutant mice have elevated very low density lipoprotein triacylglycerol and apoCIII levels. However, ligands for Rev-erb are unknown and the regulatory mechanism of Rev-erb is poorly understood. Conceivably, cofactors for Rev-erb may play an important role in the regulation of lipid metabolism. In this study, a zinc finger HIT domain-containing protein, ZNHIT-1, interacted with Rev-erbβ. ZNHIT-1 was found to be a conserved protein in eukaryotes and was highly abundant in human liver. Furthermore, ZNHIT-1 was identified as a nuclear protein. Serial truncated fragments and substitution mutations established a putative nuclear localization signal at amino acids 38-47 of ZNHIT-1. A putative ligand-binding domain of Rev-erbβ and the FxxLL motif of ZNHIT-1 were required for their interaction. Finally, ZNHIT-1 was recruited by Rev-erbβ to the apoCIII promoter and removed the Rev-erbβ-induced inhibition of apoCIII transcription. These findings demonstrate that ZNHIT-1 functions as a cofactor to regulate the activity of Rev-erbβ, and may play a role in lipid metabolism. © 2007 The Authors.

Cite

CITATION STYLE

APA

Wang, J., Li, Y., Zhang, M., Liu, Z., Wu, C., Yuan, H., … Lu, H. (2007). A zinc finger HIT domain-containing protein, ZNHIT-1, interacts with orphan nuclear hormone receptor Rev-erbβ and removes Rev-erbβ-induced inhibition of apoCIII transcription. FEBS Journal, 274(20), 5370–5381. https://doi.org/10.1111/j.1742-4658.2007.06062.x

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free