دورية أكاديمية
Monomerization and ER Relocalization of GRASP Is a Requisite for Unconventional Secretion of CFTR
| العنوان: | Monomerization and ER Relocalization of GRASP Is a Requisite for Unconventional Secretion of CFTR |
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| المساهمون: | College of Medicine, Dept. of Pharmacology, Jiyoon Kim, Shin Hye Noh, He Piao, Dong Hee Kim, Kuglae Kim, Jeong Seok Cha, Woo Young Chung, Hyun-Soo Cho, Joo Young Kim, Min Goo Lee, Kim, Dong Hee, Kim, Joo Young, Kim, Ji Yoon, Noh, Shin Hye, Lee, Min Goo |
| بيانات النشر: | Blackwell England |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | Carrier Proteins/genetics, Carrier Proteins/metabolism, Cystic Fibrosis Transmembrane Conductance Regulator/genetics, Cystic Fibrosis Transmembrane Conductance Regulator/secretion, Endoplasmic Reticulum/metabolism, Endoplasmic Reticulum Stress, Golgi Apparatus/metabolism, HEK293 Cells, HeLa Cells, Humans, Membrane Proteins/genetics, Membrane Proteins/metabolism, Mutation, Plasmids, Protein Multimerization, Protein Transport, Secretory Pathway, Transfection, CFTR, ER stress, ER-to-Golgi blockade, GRASP, unconventional secretion |
| الوصف: | Induction of endoplasmic reticulum (ER)-to-Golgi blockade or ER stress induces Golgi reassembly stacking protein (GRASP)-mediated, Golgi-independent unconventional cell-surface trafficking of the folding-deficient �봃508-cystic fibrosis transmembrane conductance regulator (CFTR). However, molecular mechanisms underlying this process remain elusive. Here, we show that phosphorylation-dependent dissociation of GRASP homotypic complexes and subsequent relocalization of GRASP to the ER play a critical role in the unconventional secretion of CFTR. Immunolocalization analyses of mammalian cells revealed that the Golgi protein GRASP55 was redistributed to the ER by stimuli that induce unconventional secretion of �봃508-CFTR, such as induction of ER-to-Golgi blockade by the Arf1 mutant. Notably, the same stimuli also induced phosphorylation of regions near the C-terminus of GRASP55 and dissociation of GRASP homomultimer complexes. Furthermore, phosphorylation-mimicking mutations of GRASP55 induced the monomerization and ER relocalization of GRASP55, and these changes were nullified by phosphorylation-inhibiting mutations. These results provide mechanistic insights into how GRASP accesses the ER-retained �봃508-CFTR and mediates the ER stress-induced unconventional secretion pathway. ; restriction |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 1398-9219 1600-0854 |
| العلاقة: | TRAFFIC; J02747; OAK-2016-04895; https://ir.ymlib.yonsei.ac.kr/handle/22282913/151879Test; T201603221; TRAFFIC, Vol.17(7) : 733-753, 2016 |
| DOI: | 10.1111/tra.12403 |
| DOI: | 10.1111/tra.12403/abstract |
| الإتاحة: | https://doi.org/10.1111/tra.12403Test https://ir.ymlib.yonsei.ac.kr/handle/22282913/151879Test |
| حقوق: | CC BY-NC-ND 2.0 KR ; https://creativecommons.org/licenses/by-nc-nd/2.0/krTest/ |
| رقم الانضمام: | edsbas.B047BAE6 |
| قاعدة البيانات: | BASE |
Full Text Finder | تدمد: | 13989219 16000854 |
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| DOI: | 10.1111/tra.12403 |