title: Human small heat shock proteins: protein interactomes of homo- and hetero-oligomeric complexes: an update.
abstract: Small heat shock proteins (sHsps) regulate a large number of fundamental cellular processes and are involved in many pathological diseases. They share complex oligomerization and phosphorylation properties allowing them to interact and modulate the activity of many client proteins. Here, the up-to date protein interactome of the ten human sHsps is presented as an illustration of their multiple cellular functions. In addition of forming homo-oligomers, some of these proteins interact whith each other and form hetero-oligomeric complexes that could bear new protein targets recognition abilities. Here, novel informations are presented on how the formation of HspB1/HspB5 complex can stimulate the activity of the oxidoresistance promoting enzyme glucose 6-phosphate dehydrogenase through its interaction with newly formed highly phosphorylated HspB1 homo-oligomers.
authors.affiliation: Apoptosis, Cancer and Development Laboratory, Lyon Cancer Research Center, INSERM U1052-CNRS UMR5286, Claude Bernard University Lyon 1, Lyon, France. parrigo@me.com
authors.forename: André-Patrick
authors.initials: AP
authors.lastname: Arrigo
mesh_terms: D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism; D050888:Heat-Shock Proteins, Small / Q000378:metabolism*; D006801:Humans; D046912:Multiprotein Complexes / Q000378:metabolism; D060066:Protein Interaction Maps; D055503:Protein Multimerization
chemical_list: D050888:Heat-Shock Proteins, Small; D046912:Multiprotein Complexes; D005954:Glucosephosphate Dehydrogenase