title: Revisiting and revising the purinosome.
abstract: Some metabolic pathway enzymes are known to organize into multi-enzyme complexes for reasons of catalytic efficiency, metabolite channeling, and other advantages of compartmentalization. It has long been an appealing prospect that de novo purine biosynthesis enzymes form such a complex, termed the "purinosome." Early work characterizing these enzymes garnered scarce but encouraging evidence for its existence. Recent investigations led to the discovery in human cell lines of purinosome bodies-cytoplasmic puncta containing transfected purine biosynthesis enzymes, which were argued to correspond to purinosomes. New discoveries challenge both the functional and physiological relevance of these bodies in favor of protein aggregation.
authors.affiliation: Center for Systems and Synthetic Biology, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA. marcotte@icmb.utexas.edu.
authors.forename: Alice
authors.initials: A
authors.lastname: Zhao
authors.forename: Mark
authors.initials: M
authors.lastname: Tsechansky
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Ellington
authors.forename: Edward M
authors.initials: EM
authors.lastname: Marcotte
mesh_terms: D003594:Cytoplasmic Granules / Q000378:metabolism; D006801:Humans; D009097:Multienzyme Complexes / Q000378:metabolism*; D011485:Protein Binding; D021381:Protein Transport; D011506:Proteins / Q000378:metabolism; D011687:Purines / Q000096:biosynthesis*
chemical_list: D009097:Multienzyme Complexes; D011506:Proteins; D011687:Purines; C030985:purine