Phosphorylation of LAMP2A by p38 MAPK couples ER stress to chaperone-mediated autophagy

Phosphorylation of LAMP2A by p38 MAPK couples ER stress to chaperone-mediated autophagy

The endoplasmic reticulum (ER) and lysosome are central to cellular stress responses, but it is unclear how ER stress is signaled to lysosomes. Here the authors show that ER stress activates chaperone-mediated autophagy (CMA) via direct phosphorylation of the CMA receptor LAMP2A by the lysosomal p38...

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Main Authors: Wenming Li, Jinqiu Zhu, Juan Dou, Hua She, Kai Tao, Haidong Xu, Qian Yang, Zixu Mao
Format: Article
Language:English
Published: Nature Publishing Group 2017-11-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-01609-x
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spelling doaj-fe92931b0c6143268e9973c5261734362021-05-11T07:09:26ZengNature Publishing GroupNature Communications2041-17232017-11-018111410.1038/s41467-017-01609-xPhosphorylation of LAMP2A by p38 MAPK couples ER stress to chaperone-mediated autophagyWenming Li0Jinqiu Zhu1Juan Dou2Hua She3Kai Tao4Haidong Xu5Qian Yang6Zixu Mao7Departments of Pharmacology and Neurology, Emory University School of MedicineDepartments of Pharmacology and Neurology, Emory University School of MedicineDepartments of Pharmacology and Neurology, Emory University School of MedicineDepartments of Pharmacology and Neurology, Emory University School of MedicineDepartment of Neurosurgery, Tangdu Hospital, The Fourth Military Medical UniversityDepartments of Pharmacology and Neurology, Emory University School of MedicineDepartment of Neurosurgery, Tangdu Hospital, The Fourth Military Medical UniversityDepartments of Pharmacology and Neurology, Emory University School of MedicineThe endoplasmic reticulum (ER) and lysosome are central to cellular stress responses, but it is unclear how ER stress is signaled to lysosomes. Here the authors show that ER stress activates chaperone-mediated autophagy (CMA) via direct phosphorylation of the CMA receptor LAMP2A by the lysosomal p38 MAPK.https://doi.org/10.1038/s41467-017-01609-x
collection DOAJ
language English
format Article
sources DOAJ
author Wenming Li
Jinqiu Zhu
Juan Dou
Hua She
Kai Tao
Haidong Xu
Qian Yang
Zixu Mao
spellingShingle Wenming Li
Jinqiu Zhu
Juan Dou
Hua She
Kai Tao
Haidong Xu
Qian Yang
Zixu Mao
Phosphorylation of LAMP2A by p38 MAPK couples ER stress to chaperone-mediated autophagy
Nature Communications
author_facet Wenming Li
Jinqiu Zhu
Juan Dou
Hua She
Kai Tao
Haidong Xu
Qian Yang
Zixu Mao
author_sort Wenming Li
title Phosphorylation of LAMP2A by p38 MAPK couples ER stress to chaperone-mediated autophagy
title_short Phosphorylation of LAMP2A by p38 MAPK couples ER stress to chaperone-mediated autophagy
title_full Phosphorylation of LAMP2A by p38 MAPK couples ER stress to chaperone-mediated autophagy
title_fullStr Phosphorylation of LAMP2A by p38 MAPK couples ER stress to chaperone-mediated autophagy
title_full_unstemmed Phosphorylation of LAMP2A by p38 MAPK couples ER stress to chaperone-mediated autophagy
title_sort phosphorylation of lamp2a by p38 mapk couples er stress to chaperone-mediated autophagy
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2017-11-01
description The endoplasmic reticulum (ER) and lysosome are central to cellular stress responses, but it is unclear how ER stress is signaled to lysosomes. Here the authors show that ER stress activates chaperone-mediated autophagy (CMA) via direct phosphorylation of the CMA receptor LAMP2A by the lysosomal p38 MAPK.
url https://doi.org/10.1038/s41467-017-01609-x
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