title: Hsp90 in non-mammalian metazoan model systems.
abstract: The molecular chaperone Hsp90 has been discovered in the heat-shock response of the fruit fly more than 30years ago. Today, it is becoming clear that Hsp90 is in the middle of a regulatory system, participating in the modulation of many essential client proteins and signaling pathways. Exerting these activities, Hsp90 works together with about a dozen of cochaperones. Due to their organismal simplicity and the possibility to influence their genetics on a large scale, many studies have addressed the function of Hsp90 in several multicellular model systems. Defined pathways involving Hsp90 client proteins have been identified in the metazoan model systems of Caenorhabditis elegans, Drosophila melanogaster and the zebrafish Danio rerio. Here, we summarize the functions of Hsp90 during muscle maintenance, development of phenotypic traits and the involvement of Hsp90 in stress responses, all of which were largely uncovered using the model organisms covered in this review. These findings highlight the many specific and general actions of the Hsp90 chaperone machinery. This article is part of a Special Issue entitled: Heat Shock Protein 90 (HSP90).
authors: Department Chemie, Technische Universitat Munchen, Garching, Germany.
authors: Veronika
authors: V
authors: Haslbeck
authors: Christoph J O
authors: CJ
authors: Kaiser
authors: Klaus
authors: K
authors: Richter
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans; D004331:Drosophila melanogaster; D018841:HSP90 Heat-Shock Proteins / Q000235:genetics* / Q000378:metabolism*; D023421:Models, Animal; D018832:Molecular Chaperones / Q000235:genetics* / Q000378:metabolism*; D015027:Zebrafish
chemical_list: D018841:HSP90 Heat-Shock Proteins; D018832:Molecular Chaperones