A TRCky TA protein delivery service snubs the UPS

In mammals, tail-anchored (TA) proteins that are posttranslationally captured by the chaperone SGTA are triaged by the BAG6 complex into one of two fates: handoff to an ER targeting factor for membrane insertion or polyubiquitination for destruction by the proteasome. In this issue, Culver and Maria...

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Detalles Bibliográficos
Autores principales: McQuown, Alexander J., Reif, Dvir, Denic, Vladimir
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Rockefeller University Press 2021
Materias:
Spotlight
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8059096/
https://www.ncbi.nlm.nih.gov/pubmed/33877288
http://dx.doi.org/10.1083/jcb.202103196
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author McQuown, Alexander J.
Reif, Dvir
Denic, Vladimir
author_facet McQuown, Alexander J.
Reif, Dvir
Denic, Vladimir
author_sort McQuown, Alexander J.
collection PubMed
description In mammals, tail-anchored (TA) proteins that are posttranslationally captured by the chaperone SGTA are triaged by the BAG6 complex into one of two fates: handoff to an ER targeting factor for membrane insertion or polyubiquitination for destruction by the proteasome. In this issue, Culver and Mariappan (2021. J. Cell Biol. https://doi.org/10.1083/jcb.202004086) show that a fraction of newly synthesized TA proteins is polyubiquitinated in HEK293 cells independently of the BAG6 complex yet evades proteasomal degradation by undergoing deubiquitination en route to becoming stably inserted into the ER membrane.
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spelling pubmed-80590962021-11-03 A TRCky TA protein delivery service snubs the UPS McQuown, Alexander J. Reif, Dvir Denic, Vladimir J Cell Biol Spotlight In mammals, tail-anchored (TA) proteins that are posttranslationally captured by the chaperone SGTA are triaged by the BAG6 complex into one of two fates: handoff to an ER targeting factor for membrane insertion or polyubiquitination for destruction by the proteasome. In this issue, Culver and Mariappan (2021. J. Cell Biol. https://doi.org/10.1083/jcb.202004086) show that a fraction of newly synthesized TA proteins is polyubiquitinated in HEK293 cells independently of the BAG6 complex yet evades proteasomal degradation by undergoing deubiquitination en route to becoming stably inserted into the ER membrane. Rockefeller University Press 2021-04-20 /pmc/articles/PMC8059096/ /pubmed/33877288 http://dx.doi.org/10.1083/jcb.202103196 Text en © 2021 McQuown et al. http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Spotlight
McQuown, Alexander J.
Reif, Dvir
Denic, Vladimir
A TRCky TA protein delivery service snubs the UPS
title A TRCky TA protein delivery service snubs the UPS
title_full A TRCky TA protein delivery service snubs the UPS
title_fullStr A TRCky TA protein delivery service snubs the UPS
title_full_unstemmed A TRCky TA protein delivery service snubs the UPS
title_short A TRCky TA protein delivery service snubs the UPS
title_sort trcky ta protein delivery service snubs the ups
topic Spotlight
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8059096/
https://www.ncbi.nlm.nih.gov/pubmed/33877288
http://dx.doi.org/10.1083/jcb.202103196
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