ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation

The chaperone Hsp70 has a dual role, promoting both protein refolding and protein degradation. Seo and Park et al. show that Hsp70 acetylation enhances protein refolding after stress, and that subsequent deacetylation progressively promotes ubiquitin ligase binding and protein degradation.

Guardado en:
Detalles Bibliográficos
Autores principales: Ji Hae Seo, Ji-Hyeon Park, Eun Ji Lee, Tam Thuy Lu Vo, Hoon Choi, Jun Yong Kim, Jae Kyung Jang, Hee-Jun Wee, Hye Shin Lee, Se Hwan Jang, Zee Yong Park, Jaeho Jeong, Kong-Joo Lee, Seung-Hyeon Seok, Jin Young Park, Bong Jin Lee, Mi-Ni Lee, Goo Taeg Oh, Kyu-Won Kim
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2016
Materias:
Q
Acceso en línea:https://doaj.org/article/bbe3b18cb62b4560996ac9f25bb15fdb
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:bbe3b18cb62b4560996ac9f25bb15fdb
record_format dspace
spelling oai:doaj.org-article:bbe3b18cb62b4560996ac9f25bb15fdb2021-12-02T14:39:29ZARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation10.1038/ncomms128822041-1723https://doaj.org/article/bbe3b18cb62b4560996ac9f25bb15fdb2016-10-01T00:00:00Zhttps://doi.org/10.1038/ncomms12882https://doaj.org/toc/2041-1723The chaperone Hsp70 has a dual role, promoting both protein refolding and protein degradation. Seo and Park et al. show that Hsp70 acetylation enhances protein refolding after stress, and that subsequent deacetylation progressively promotes ubiquitin ligase binding and protein degradation.Ji Hae SeoJi-Hyeon ParkEun Ji LeeTam Thuy Lu VoHoon ChoiJun Yong KimJae Kyung JangHee-Jun WeeHye Shin LeeSe Hwan JangZee Yong ParkJaeho JeongKong-Joo LeeSeung-Hyeon SeokJin Young ParkBong Jin LeeMi-Ni LeeGoo Taeg OhKyu-Won KimNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-14 (2016)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Ji Hae Seo
Ji-Hyeon Park
Eun Ji Lee
Tam Thuy Lu Vo
Hoon Choi
Jun Yong Kim
Jae Kyung Jang
Hee-Jun Wee
Hye Shin Lee
Se Hwan Jang
Zee Yong Park
Jaeho Jeong
Kong-Joo Lee
Seung-Hyeon Seok
Jin Young Park
Bong Jin Lee
Mi-Ni Lee
Goo Taeg Oh
Kyu-Won Kim
ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation
description The chaperone Hsp70 has a dual role, promoting both protein refolding and protein degradation. Seo and Park et al. show that Hsp70 acetylation enhances protein refolding after stress, and that subsequent deacetylation progressively promotes ubiquitin ligase binding and protein degradation.
format article
author Ji Hae Seo
Ji-Hyeon Park
Eun Ji Lee
Tam Thuy Lu Vo
Hoon Choi
Jun Yong Kim
Jae Kyung Jang
Hee-Jun Wee
Hye Shin Lee
Se Hwan Jang
Zee Yong Park
Jaeho Jeong
Kong-Joo Lee
Seung-Hyeon Seok
Jin Young Park
Bong Jin Lee
Mi-Ni Lee
Goo Taeg Oh
Kyu-Won Kim
author_facet Ji Hae Seo
Ji-Hyeon Park
Eun Ji Lee
Tam Thuy Lu Vo
Hoon Choi
Jun Yong Kim
Jae Kyung Jang
Hee-Jun Wee
Hye Shin Lee
Se Hwan Jang
Zee Yong Park
Jaeho Jeong
Kong-Joo Lee
Seung-Hyeon Seok
Jin Young Park
Bong Jin Lee
Mi-Ni Lee
Goo Taeg Oh
Kyu-Won Kim
author_sort Ji Hae Seo
title ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation
title_short ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation
title_full ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation
title_fullStr ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation
title_full_unstemmed ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation
title_sort ard1-mediated hsp70 acetylation balances stress-induced protein refolding and degradation
publisher Nature Portfolio
publishDate 2016
url https://doaj.org/article/bbe3b18cb62b4560996ac9f25bb15fdb
work_keys_str_mv AT jihaeseo ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT jihyeonpark ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT eunjilee ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT tamthuyluvo ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT hoonchoi ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT junyongkim ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT jaekyungjang ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT heejunwee ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT hyeshinlee ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT sehwanjang ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT zeeyongpark ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT jaehojeong ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT kongjoolee ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT seunghyeonseok ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT jinyoungpark ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT bongjinlee ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT minilee ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT gootaegoh ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
AT kyuwonkim ard1mediatedhsp70acetylationbalancesstressinducedproteinrefoldinganddegradation
_version_ 1718390614240788480