title: Structural analysis of glyceraldehyde-3-phosphate dehydrogenase functional diversity.
abstract: Multifunctional proteins provide a new mechanism to expand exponentially cell information and capability beyond that indicated by conventional gene analyses. As such, examination of their structure-function relationships provides a means to define the mechanisms through which cells accomplish critical yet disparate activities required for cell viability and survival. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) may be considered the quintessential multidimensional protein which exhibits a variety of functions unrelated to its classical role in energy production. This review discusses new insights into the structure-function mechanisms through which defined GAPDH amino acid domains are utilized for its diverse activities, the importance of its post-translational modification, and, intriguingly, the logic inherent in the presence or the absence of specific signaling domains.
authors.affiliation: Department of Pharmacology, Temple University School of Medicine, Philadelphia, PA 19140, United States. Electronic address: msirover@temple.edu.
authors.forename: Michael A
authors.initials: MA
authors.lastname: Sirover
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data
chemical_list: D005987:Glyceraldehyde-3-Phosphate Dehydrogenases
keywords: Amino acid domains; Glyceraldehyde-3-phosphate dehydrogenase; Multifunctional protein; Post-translational modification; mRNA stability