The Erv41–Erv46 complex serves as a retrograde receptor to retrieve escaped ER proteins

Shibuya, Aya; Margulis, Neil G.; Christiano, Romain; Walther, Tobias C.; Barlowe, Charles

doi:10.1083/jcb.201408024

Cited by 41 publications

(47 citation statements)

References 70 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The results indicate how ER residency may rely on the superposition of the retention and retrieval processes. Although our experiments focus on KDEL-mediated retrieval, it seems likely that additional retrieval systems, involving Rer1 and Erv41-Erv46, will likewise be supported by COPII-dependent retention (Sato et al, 1995; Shibuya et al, 2015). Finally, the saturation of the KDEL system that is indicated by our results in Figure 5A has relevance to the mechanism by which 4-PBA restores trafficking of misfolded LDL receptor.…”

Section: Resultsmentioning

confidence: 99%

ER retention is imposed by COPII protein sorting and attenuated by 4-phenylbutyrate

Goldberg

2017

eLife

View full text Add to dashboard Cite

Native cargo proteins exit the endoplasmic reticulum (ER) in COPII-coated vesicles, whereas resident and misfolded proteins are substantially excluded from vesicles by a retention mechanism that remains unresolved. We probed the ER retention process using the proteostasis regulator 4-phenylbutyrate (4-PBA), which we show targets COPII protein to reduce the stringency of retention. 4-PBA competes with p24 proteins to bind COPII. When p24 protein uptake is blocked, COPII vesicles package resident proteins and an ER-trapped mutant LDL receptor. We further show that 4-PBA triggers the secretion of a KDEL-tagged luminal resident, implying that a compromised retention mechanism causes saturation of the KDEL retrieval system. The results indicate that stringent ER retention requires the COPII coat machinery to actively sort biosynthetic cargo from diffusible misfolded and resident ER proteins.DOI: http://dx.doi.org/10.7554/eLife.26624.001

show abstract

Section: Resultsmentioning

confidence: 99%

ER retention is imposed by COPII protein sorting and attenuated by 4-phenylbutyrate

Goldberg

2017

eLife

View full text Add to dashboard Cite

show abstract

“…More recently, a third class of retrograde sorting receptor was identified and characterized through proteomic analysis of ER-derived transport vesicles (Otte et al 2001). The Erv41-Erv46 complex is required for ER localization of soluble ER-resident proteins that lack a C-terminal KDEL motif, including glucosidase I and the prolyl isomerase FKBP-13 (Shibuya et al 2015). The signal recognized in these soluble cargo remains to be determined.…”

Section: Retrograde Sorting Signals and Receptorsmentioning

confidence: 98%

Cargo Capture and Bulk Flow in the Early Secretory Pathway

Barlowe

Helenius

2016

Annu. Rev. Cell Dev. Biol.

Self Cite

181

191

View full text Add to dashboard Cite

Transport of newly synthesized proteins from the endoplasmic reticulum (ER) to the Golgi complex is highly selective. As a general rule, such transport is limited to soluble and membrane-associated secretory proteins that have reached properly folded and assembled conformations. To secure the efficiency, fidelity, and control of this crucial transport step, cells use a combination of mechanisms. The mechanisms are based on selective retention of proteins in the ER to prevent uptake into transport vesicles, on selective capture of proteins in COPII carrier vesicles, on inclusion of proteins in these vesicles by default as part of fluid and membrane bulk flow, and on selective retrieval of proteins from post-ER compartments by retrograde vesicle transport.

show abstract

“…Some proteins, such as Rer1, Vps74, the Erv41-46 complex (Shibuya et al, 2015) and the KDEL receptor, bind COPI and serve as adaptors, mediating sorting of cargo into COPI-coated vesicles. Rer1 recognizes retrieval signals within the transmembrane domain of many proteins, while Vps74 -a member of the GOLPH3 familyrecognizes sorting signals in the cytoplasmic domain of many Golgi-localized glycosyltransferases (Eckert et al, 2014;Sato et al, 2001;Tu et al, 2008Tu et al, , 2012.…”

Section: Cargo Recognition By Copimentioning

confidence: 99%

Formation of COPI-coated vesicles at a glance

Arakel

Schwappach

2018

Journal of Cell Science

103

106

View full text Add to dashboard Cite

show abstract

The Erv41–Erv46 complex serves as a retrograde receptor to retrieve escaped ER proteins

Abstract: pH-dependent receptor binding of specific cargo by the Erv41–Erv46 complex in Golgi compartments identifies escaped ER resident proteins that are then returned to the ER in COPI vesicles.

Cited by 41 publications

References 70 publications

ER retention is imposed by COPII protein sorting and attenuated by 4-phenylbutyrate

ER retention is imposed by COPII protein sorting and attenuated by 4-phenylbutyrate

Cargo Capture and Bulk Flow in the Early Secretory Pathway

Formation of COPI-coated vesicles at a glance

Contact Info

Product

Resources

About