HSP90: the Rosetta stone for cellular protein dynamics?
The Hsp90 proteomic network is expansive and includes a variety of cell processes operating within the cytoplasm and nucleoplasm. Though the functional significance of the extensive interactions has not been defined, we suggest that the Hsp90 molecular chaperone machinery promotes dynamic behaviors for client proteins that is critical to achieve homeostasis. A general rapid action by cell factors would permit both proper assembly of biological complexes and efficient transitions between distinct structures. Here, we describe why the properties that are inherent to molecular chaperones place these proteins in a unique position to drive the dynamic cellular environment.
Dezwaan
Diane C
DC
Department of Cell and Developmental Biology, University of Illinois, Urbana, Illinois, USA.
Freeman
Brian C
BC
D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006706:Homeostasis / Q000235:genetics*; D053858:Metabolic Networks and Pathways / Q000235:genetics*; D008954:Models, Biological; D018832:Molecular Chaperones / Q000378:metabolism*; D046912:Multiprotein Complexes / Q000378:metabolism*; D016615:Telomere / Q000502:physiology*
D018841:HSP90 Heat-Shock Proteins; D018832:Molecular Chaperones; D046912:Multiprotein Complexes