A nonconventional role of molecular chaperones: involvement in the cytoarchitecture.
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.
Csermely
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Department of Medical Chemistry, Semmelweis University, H-1444 Budapest, and the Biorex Corporation, H-8200 Veszprém, Hungary.
D000818:Animals; D002468:Cell Physiological Phenomena; D002477:Cells / Q000166:cytology*; D006801:Humans; D018832:Molecular Chaperones / Q000502:physiology*; D017510:Protein Folding
D018832:Molecular Chaperones