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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Main Authors:	Jinsei Jung, Jiyoon Kim, Shin Hye Roh, Ikhyun Jun, Robert D. Sampson, Heon Yung Gee, Jae Young Choi, Min Goo Lee
Format:	Article
Language:	English
Published:	Nature Publishing Group 2016-04-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/ncomms11386

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spelling	doaj-aa16d7f6f34648b89129e2fecc7a812a2021-05-11T10:43:38ZengNature Publishing GroupNature Communications2041-17232016-04-017111510.1038/ncomms11386The HSP70 co-chaperone DNAJC14 targets misfolded pendrin for unconventional protein secretionJinsei Jung0Jiyoon Kim1Shin Hye Roh2Ikhyun Jun3Robert D. Sampson4Heon Yung Gee5Jae Young Choi6Min Goo Lee7Department of Pharmacology and Brain Korea 21 Project for Medical Sciences, Yonsei University College of MedicineDepartment of Pharmacology and Brain Korea 21 Project for Medical Sciences, Yonsei University College of MedicineDepartment of Pharmacology and Brain Korea 21 Project for Medical Sciences, Yonsei University College of MedicineDepartment of Pharmacology and Brain Korea 21 Project for Medical Sciences, Yonsei University College of MedicineDepartment of Pharmacology and Brain Korea 21 Project for Medical Sciences, Yonsei University College of MedicineDepartment of Pharmacology and Brain Korea 21 Project for Medical Sciences, Yonsei University College of MedicineDepartment of Otorhinolaryngology, Yonsei University College of MedicineDepartment of Pharmacology and Brain Korea 21 Project for Medical Sciences, Yonsei University College of MedicineMutations 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.https://doi.org/10.1038/ncomms11386
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Jinsei Jung Jiyoon Kim Shin Hye Roh Ikhyun Jun Robert D. Sampson Heon Yung Gee Jae Young Choi Min Goo Lee
spellingShingle	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 Nature Communications
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 Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2016-04-01
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.
url	https://doi.org/10.1038/ncomms11386
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The HSP70 co-chaperone DNAJC14 targets misfolded pendrin for unconventional protein secretion

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