A nonconventional role of molecular chaperones: Involvement in the cytoarchitecture

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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.

Original languageEnglish
Pages (from-to)123-126
Number of pages4
JournalNews in Physiological Sciences
Volume16
Issue number3
Publication statusPublished - Jun 1 2001

ASJC Scopus subject areas

  • Physiology

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