Endoplasmic reticulum-associated degradation and protein quality control

Zacchi, L.F., Caramelo, J.J., McCracken, A.A. and Brodsky, J.L. (2016). Endoplasmic reticulum-associated degradation and protein quality control. In Ralph A. Bradshaw and Philip D. Stahl (Ed.), Encyclopedia of cell biology (pp. 596-611) Waltham, MA, United States: Academic Press.

Author Zacchi, L.F.
Caramelo, J.J.
McCracken, A.A.
Brodsky, J.L.
Title of chapter Endoplasmic reticulum-associated degradation and protein quality control
Title of book Encyclopedia of cell biology
Place of Publication Waltham, MA, United States
Publisher Academic Press
Publication Year 2016
Sub-type Chapter in reference work, encyclopaedia, manual or handbook
Open Access Status Not Open Access
Year available 2016
ISBN 9780123944474
Editor Ralph A. Bradshaw
Philip D. Stahl
Volume number 1
Start page 596
End page 611
Total pages 16
Collection year 2017
Language eng
Abstract/Summary Approximately one-third of all polypeptides synthesized in eukaryotes are targeted to the endoplasmic reticulum (ER), and once associated with this compartment they are chemically modified. The folding status of the resulting nascent proteins is then surveyed by molecular chaperones and lectins. To clear the ER of dead-end products, proteins that fail quality control are routed to the cytosol and degraded via ER-associated degradation (ERAD). Although many ERAD-requiring factors have been identified and a basic understanding of this pathway has been achieved, numerous questions remain on the mechanisms that lead to the selection and delivery of ERAD substrates.
Keyword Endoplasmic reticulum-associated degradation (ERAD)
Endoplasmic reticulum (ER)
Cytosolic destruction
Selective degradation
Q-Index Code BX
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Book Chapter
Collections: HERDC Pre-Audit
School of Chemistry and Molecular Biosciences
Version Filter Type
Citation counts: Google Scholar Search Google Scholar
Created: Wed, 13 Apr 2016, 18:28:08 EST by Lucia Zacchi on behalf of School of Chemistry & Molecular Biosciences