title: Proteasome dynamics.
abstract: Proteasomes are highly conserved multisubunit protease complexes and occur in the cyto- and nucleoplasm of eukaryotic cells. In dividing cells proteasomes exist as holoenzymes and primarily localize in the nucleus. During quiescence they dissociate into proteolytic core and regulatory complexes and are sequestered into motile cytosolic clusters. Proteasome clusters rapidly clear upon the exit from quiescence, where proteasome core and regulatory complexes reassemble and localize to the nucleus again. The mechanisms underlying proteasome transport and assembly are not yet understood. Here, I summarize our present knowledge about nuclear transport and assembly of proteasomes in yeast and project our studies in this eukaryotic model organism to the mammalian cell system. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System. Guest Editors: Thomas Sommer and Dieter H. Wolf.
authors.affiliation: University of Toronto, Medical Sciences Building, Department of Biochemistry, 1 King's College Circle, Toronto, Ontario, Canada M5S 1A8. Electronic address: cordula.enenkel@utoronto.ca.
authors.forename: Cordula
authors.initials: C
authors.lastname: Enenkel
mesh_terms: D021581:Active Transport, Cell Nucleus / Q000235:genetics; D000818:Animals; D002455:Cell Division / Q000502:physiology; D002467:Cell Nucleus / Q000378:metabolism; D014644:Genetic Variation / Q000502:physiology; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D046988:Proteasome Endopeptidase Complex
keywords: Nuclear protein degradation; Nuclear transport; Proteasome assembly; Proteasome storage granuli; Quiescence; Ubiquitin-proteasome system