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

   


Authors: Ma, W.; Goldberg, E.; Goldberg, J.
Article Title: ER retention is imposed by COPII protein sorting and attenuated by 4-phenylbutyrate
Abstract: 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. © Ma et al.
Journal Title: eLife
Volume: 6
ISSN: 2050-084X
Publisher: eLife Sciences Publications Ltd.  
Date Published: 2017-06-08
Start Page: e26624
Language: English
DOI: 10.7554/eLife.26624
PROVIDER: scopus
PMCID: PMC5464768
PUBMED: 28594326
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-85023602348&doi=10.7554%2feLife.26624&partnerID=40&md5=c0998b9553c1e2791eae343f68797d11
Notes: Article -- Export Date: 2 August 2017 -- Source: Scopus
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MSK Authors
  1. Jonathan D Goldberg
    22 Goldberg
  2. Elena Goldberg
    6 Goldberg
  3. Wenfu Ma
    4 Ma
  4. Weirui Ma
    6 Ma
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