title: On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: biochemical mechanisms and regulatory control.
abstract: BACKGROUND
  New studies provide evidence that glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is not simply a classical glycolytic protein of little interest. Instead, it is a multifunctional protein with significant activity in a number of fundamental cell pathways. GAPDH is a highly conserved gene and protein, with a single mRNA transcribed from a unique gene. Control mechanisms must exist which regulate its functional diversity.
  
  
  METHODS
  This review focuses on new, timely studies defining not only its diverse activities but also those which define the regulatory mechanisms through which those functions may be controlled. The reader is referred to the author's prior review for the consideration of past reports which first indicated GAPDH multiple activities (Sirover, Biochim. Biophys. Acta 1432 (1999) 159-184.)
  
  
  CONCLUSIONS
  These investigations demonstrate fundamental roles of GAPDH in vivo, dynamic changes in its subcellular localization, and the importance of posttranslational modifications as well as protein:protein interactions as regulatory control mechanisms.
  
  
  CONCLUSIONS
  GAPDH is the prototype "moonlighting" protein which exhibits activities distinct from their classically identified functions. Their participation in diverse cell pathways is essential. Regulatory mechanisms exist which control those diverse activities as well as changes in their subcellular localization as a consequence of those new functions.
authors.affiliation: Department of Pharmacology, Temple University School of Medicine, Philadelphia, PA 19140, USA. msirover@temple.edu
authors.forename: Michael A
authors.initials: MA
authors.lastname: Sirover
mesh_terms: D000818:Animals; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D011499:Protein Processing, Post-Translational / Q000502:physiology
chemical_list: D005987:Glyceraldehyde-3-Phosphate Dehydrogenases