D-Glyceraldehyde-3-Phosphate Dehydrogenase Structure and Function

• Published in: Macromolecular Protein Complexes Vol. 83; pp. 413 - 453
• Main Authors: White, Michael R., Garcin, Elsa D.
• Format: Book Chapter Journal Article
• Language: English
• Published: Switzerland Springer International Publishing AG 01.01.2017; Springer International Publishing
• Series: Subcellular Biochemistry
• Subjects: Animals; GAPDH; Glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde-3-Phosphate Dehydrogenases - chemistry; Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism; Glycolysis; Humans; Interfaces; Localization; Multifunctional; NAD; Oligomerization; Post-translational modifications; Protein Processing, Post-Translational; Proteins; Structural; Interfaces; NAD; Oligomerization; Post-translational modifications; Structural; Glyceraldehyde-3-phosphate dehydrogenase; Localization; GAPDH; Multifunctional
• ISBN: 9783319465012; 3319465015
• ISSN: 0306-0225; 2542-8810
• DOI: 10.1007/978-3-319-46503-6_15

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 oligomerizationoligomerization, biomolecular interactions, post-translational modificationspost-translational modifications, and variations in subcellular localizationlocalization. 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.