GAPDH as a model non-canonical AU-rich RNA binding protein.

Affiliation

University of Maryland Baltimore County, Department of Chemistry and Biochemistry, 1000 Hilltop Circle, Baltimore, MD, 21250, USA. Electronic address: [Email]

Abstract

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays a key role in glycolysis but is also known for its involvement in a myriad of extra-glycolytic functions. While GAPDH is not the only enzyme with established moonlighting roles, it shows great diversity in terms of its functions, cellular localizations, protein partners, and post-translational modifications. This review focuses on GAPDH's role as a non-canonical RNA binding protein to regulate the stability and translation of cellular mRNAs. Despite the clear involvement of GAPDH in gene expression regulation, how and where GAPDH binds to its RNA targets is still unknown. In addition, the mechanism by which GAPDH switches among its various cellular functions is also unknown. This review will summarize our current understanding of GAPDH-mediated regulation of RNA function.

Keywords

GAPDH,Metabolism,Post-transcriptional regulation,RNA-binding protein,Translational repressor,mRNA stability,

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