The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
ERdj5 Is Required as a Disulfide Reductase for Degradation of Misfolded Proteins in the ER
Abstract
Membrane and secretory proteins cotranslationally enter and are folded in the endoplasmic reticulum (ER). Misfolded or unassembled proteins are discarded by a process known as ER-associated degradation (ERAD), which involves their retrotranslocation into the cytosol. ERAD substrates frequently contain disulfide bonds that must be cleaved before their retrotranslocation. Here, we found that an ER-resident protein ERdj5 had a reductase activity, cleaved the disulfide bonds of misfolded proteins, and accelerated ERAD through its physical and functional associations with EDEM (ER degradation–enhancing α-mannosidase–like protein) and an ER-resident chaperone BiP. Thus, ERdj5 is a member of a supramolecular ERAD complex that recognizes and unfolds misfolded proteins for their efficient retrotranslocation.
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Cites
Quality control in the endoplasmic reticulum
Ellgaard, L., & Helenius, A. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1052 · Cited by 2,126
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
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Role of EDEM in the Release of Misfolded Glycoproteins from the Calnexin Cycle
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A novel ER α‐mannosidase‐like protein accelerates ER‐associated degradation
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Self-citationEDEM As an Acceptor of Terminally Misfolded Glycoproteins Released from Calnexin
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Self-citationOda, Y., Okada, T., Yoshida, H., Kaufman, R. J., Nagata, K., & Mori, K. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200507057 · Cited by 379
Self-citationManipulation of oxidative protein folding and PDI redox state in mammalian cells
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Cited by
One step at a time: endoplasmic reticulum-associated degradation
Vembar, S. S., & Brodsky, J. L. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2546 · Cited by 1,299
Santos, C. X. C., Tanaka, L. Y., Wosniak, J., & Laurindo, F. R. M. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2625 · Cited by 572
Protein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms
Buchberger, A., Bukau, B., & Sommer, T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.001 · Cited by 483
HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum
Wang, J., Lee, J., Liem, D., & Ping, P. (2017) · Gene · doi:10.1016/j.gene.2017.03.005 · Cited by 308
Protein quality control in the ER: The recognition of misfolded proteins
Määttänen, P., Gehring, K., Bergeron, J. J. M., & Thomas, D. Y. (2010) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2010.03.006 · Cited by 284
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Metadata
- Authors
- Ushioda, R., Hoseki, J., Araki, K., Jansen, G., Thomas, D. Y., & Nagata, K.
- Venue
- Science
- Published
- 2008-07-25
- Volume
- 321
- Issue
- 5888
- Pages
- 569-572
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2065278356
- Cited by
- 401
- References
- 18
- FWCI
- 14.06
- Type
- journal article
- Language
- en
- Open access
- closed
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- Ushioda, R., Hoseki, J., Araki, K., Jansen, G., Thomas, D. Y., & Nagata, K. (2008). ERdj5 Is Required as a Disulfide Reductase for Degradation of Misfolded Proteins in the ER. Science. https://doi.org/10.1126/science.1159293
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