The HSP70 co-chaperone DNAJC14 targets misfolded pendrin for unconventional protein secretion

Mutations in pendrin, a plasma membrane transporter, lead to Pendred syndrome, which is associated with hearing loss. Here, Jung et al. show that cell-surface expression of a mutated form of pendrin can be restored by blocking ER-to-Golgi traffic and triggering a DNAJC14 dependent unconventional sec...

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Autores principales:	Jinsei Jung, Jiyoon Kim, Shin Hye Roh, Ikhyun Jun, Robert D. Sampson, Heon Yung Gee, Jae Young Choi, Min Goo Lee
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/aa16d7f6f34648b89129e2fecc7a812a
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spelling	oai:doaj.org-article:aa16d7f6f34648b89129e2fecc7a812a2021-12-02T15:34:31ZThe HSP70 co-chaperone DNAJC14 targets misfolded pendrin for unconventional protein secretion10.1038/ncomms113862041-1723https://doaj.org/article/aa16d7f6f34648b89129e2fecc7a812a2016-04-01T00:00:00Zhttps://doi.org/10.1038/ncomms11386https://doaj.org/toc/2041-1723Mutations in pendrin, a plasma membrane transporter, lead to Pendred syndrome, which is associated with hearing loss. Here, Jung et al. show that cell-surface expression of a mutated form of pendrin can be restored by blocking ER-to-Golgi traffic and triggering a DNAJC14 dependent unconventional secretion pathway.Jinsei JungJiyoon KimShin Hye RohIkhyun JunRobert D. SampsonHeon Yung GeeJae Young ChoiMin Goo LeeNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-15 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jinsei Jung Jiyoon Kim Shin Hye Roh Ikhyun Jun Robert D. Sampson Heon Yung Gee Jae Young Choi Min Goo Lee The HSP70 co-chaperone DNAJC14 targets misfolded pendrin for unconventional protein secretion
description	Mutations in pendrin, a plasma membrane transporter, lead to Pendred syndrome, which is associated with hearing loss. Here, Jung et al. show that cell-surface expression of a mutated form of pendrin can be restored by blocking ER-to-Golgi traffic and triggering a DNAJC14 dependent unconventional secretion pathway.
format	article
author	Jinsei Jung Jiyoon Kim Shin Hye Roh Ikhyun Jun Robert D. Sampson Heon Yung Gee Jae Young Choi Min Goo Lee
author_facet	Jinsei Jung Jiyoon Kim Shin Hye Roh Ikhyun Jun Robert D. Sampson Heon Yung Gee Jae Young Choi Min Goo Lee
author_sort	Jinsei Jung
title	The HSP70 co-chaperone DNAJC14 targets misfolded pendrin for unconventional protein secretion
title_short	The HSP70 co-chaperone DNAJC14 targets misfolded pendrin for unconventional protein secretion
title_full	The HSP70 co-chaperone DNAJC14 targets misfolded pendrin for unconventional protein secretion
title_fullStr	The HSP70 co-chaperone DNAJC14 targets misfolded pendrin for unconventional protein secretion
title_full_unstemmed	The HSP70 co-chaperone DNAJC14 targets misfolded pendrin for unconventional protein secretion
title_sort	hsp70 co-chaperone dnajc14 targets misfolded pendrin for unconventional protein secretion
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/aa16d7f6f34648b89129e2fecc7a812a
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The HSP70 co-chaperone DNAJC14 targets misfolded pendrin for unconventional protein secretion

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