Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH): The Quintessential Moonlighting Protein in Normal Cell Function and in Human Disease

Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH): The Quintessential Moonlighting Protein in Normal Cell Function and in Human Disease examines the biochemical protein interactions of the multi-dimensional protein GAPDH, further considering the regulatory mechanisms through which cells control their functional diversity.

This protein’s diverse activities range from nuclear tRNA export and the maintenance of genomic integrity, to cytoplasmic post-transcriptional control of gene expression and receptor mediated cell signaling, to membrane facilitation of iron metabolism, trafficking and fusion.

This book will be of great interest to basic scientists, clinicians and students, including molecular and cell biologists, immunologists, pathologists and clinical researchers who are interested in the biochemistry of GAPDH in health and disease.

Contextualizes how GAPDH is utilized by cells in vivoProvides detailed insight into GAPDH post-translational modifications, including functional diversity and its subcellular localizationIncludes forward-thinking exposition on tough topics, such as the exploration of how GAPDG performs functions, how it decides where it should be present and requisite structural requirements

Section I.  Moonlighting GAPDH in Normal Cell Function 1. Transcriptional Expression 2. Post-translational mRNA Regulation 3. Iron Metabolism 4. Membrane Trafficking 5. Maintenance of DNA Integrity 6. GAPDH and Neural Transmission 7. GAPDH and Cell Proliferation

Section II. Physiological Stress and GAPDH Functional Diversity 1. GAPDH and Oxidative Stress: Nitric Oxide, apoptosis and heme metabolism 2. GAPDH and Hypoxia 3. GAPDH and Ischemia. Ischemia may be defined as a restriction in blood supply to tissues resulting in oxygen deprivation. Recent studies indicate that moonlighting GAPDH may be specifically regulated as a function of ischemic stress. This includes its role in receptor mediated glutamate exocytosis and its intracellular interaction with the p53 protein. The former regulates AMPAR action while the latter involves the formation of a GAPDH:p53 protein-protein complex as well as post-translational modification of the p53 protein.

Section III. The Pathology of GAPDH Functional Diversity 1. GAPDH and Age-Related Neurodegenerative Disease 2. Moonlighting GAPDH and Cancer Development 3. Functional Diversity of GAPDH in Infection and Immunity

Section IV. The Pharmacology of Moonlighting GAPDH

Section V. Discussion