title: D-Glyceraldehyde-3-Phosphate Dehydrogenase Structure and Function.
abstract: Aside from its well-established role in glycolysis, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been shown to possess many key functions in cells. These functions are regulated by protein oligomerization , biomolecular interactions, post-translational modifications , and variations in subcellular localization . Several GAPDH functions and regulatory mechanisms overlap with one another and converge around its role in intermediary metabolism. Several structural determinants of the protein dictate its function and regulation. GAPDH is ubiquitously expressed and is found in all domains of life. GAPDH has been implicated in many diseases, including those of pathogenic, cardiovascular, degenerative, diabetic, and tumorigenic origins. Understanding the mechanisms by which GAPDH can switch between its functions and how these functions are regulated can provide insights into ways the protein can be modulated for therapeutic outcomes.
authors.affiliation: Department of Structural Biology, St. Jude Children's Research Hospital, 262 Danny Thomas Place, Memphis, TN, 28105, USA. whitem2@umbc.edu.
authors.forename: Michael R
authors.initials: MR
authors.lastname: White
authors.affiliation: Department of Chemistry and Biochemistry, University of Maryland Baltimore County, 1000 Hilltop Circle, Baltimore, MD, 21250, USA.
authors.forename: Elsa D
authors.initials: ED
authors.lastname: Garcin
mesh_terms: D000818:Animals; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism*; D006019:Glycolysis; D006801:Humans; D011499:Protein Processing, Post-Translational
chemical_list: D005987:Glyceraldehyde-3-Phosphate Dehydrogenases
keywords: GAPDH; Glyceraldehyde-3-phosphate dehydrogenase; Interfaces; Localization; Multifunctional; NAD+; Oligomerization; Post-translational modifications; Structural