title: Déjà vu with a twist: transglutaminases in bioenergetics and transcriptional dysfunction in Huntington's disease.
abstract: The article by McConoughey et al in the current issue of EMBO Molecular Medicine examines the contribution of transglutaminase 2 (TG2) to Huntington's disease (HD) pathogenesis. The authors find that TG2 inhibition can ameliorate HD neurodegeneration, and thereby elevate the status of transglutaminases (TGs) to a major therapeutic target-not because of their well-known activity in mutant protein aggregation, but instead based upon their ability to epigenetically modulate transcription and energy production. While the reintroduction of TG inhibition as a therapy for HD may evoke feelings of déjà vu, the outcome this time around could go in a dramatically different direction.
authors: Division of Genetics, Department of Pediatrics, University of California, San Diego - La Jolla, CA, USA.
authors: Parsa
authors: P
authors: Kazemi-Esfarjani
authors: Albert R
authors: AR
authors: La Spada
mesh_terms: D000818:Animals; D004195:Disease Models, Animal; D004330:Drosophila; D004734:Energy Metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology; D019204:GTP-Binding Proteins / Q000037:antagonists & inhibitors* / Q000235:genetics / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D006801:Humans; D006816:Huntington Disease / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D010455:Peptides / Q000494:pharmacology; D011073:Polyamines / Q000378:metabolism; D000091345:Protein Glutamine gamma Glutamyltransferase 2; D014158:Transcription, Genetic; D011503:Transglutaminases / Q000037:antagonists & inhibitors* / Q000235:genetics / Q000378:metabolism
chemical_list: D004791:Enzyme Inhibitors; D006657:Histones; D010455:Peptides; D011073:Polyamines; D000091345:Protein Glutamine gamma Glutamyltransferase 2; D011503:Transglutaminases; D019204:GTP-Binding Proteins