title: A nonconventional role of molecular chaperones: involvement in the cytoarchitecture.
abstract: A hallmark of chaperone action is assistance in protein folding. Indeed, folding of nascent prokaryotic proteins proceeds mostly as a chaperone-assisted, posttranslational event. On the contrary, in nonstressed eukaryotic cells folding-related tasks of eukaryotic chaperones are restricted to a subset of proteins, and "jobless" chaperones may form an extension of the cytoarchitecture, facilitating intracellular traffic of proteins and other macromolecules.
authors.affiliation: Department of Medical Chemistry, Semmelweis University, H-1444 Budapest, and the Biorex Corporation, H-8200 Veszprém, Hungary.
authors.forename: P
authors.initials: P
authors.lastname: Csermely
mesh_terms: D000818:Animals; D002468:Cell Physiological Phenomena; D002477:Cells / Q000166:cytology*; D006801:Humans; D018832:Molecular Chaperones / Q000502:physiology*; D017510:Protein Folding
chemical_list: D018832:Molecular Chaperones