Cargando…
DjA1 maintains Golgi integrity via interaction with GRASP65
In mammalian cells, the Golgi reassembly stacking protein of 65 kDa (GRASP65) has been implicated in both Golgi stacking and ribbon linking by forming trans-oligomers. To better understand its function and regulation, we used biochemical methods to identify the DnaJ homolog subfamily A member 1 (DjA...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6594443/ https://www.ncbi.nlm.nih.gov/pubmed/30566031 http://dx.doi.org/10.1091/mbc.E18-10-0613 |
_version_ | 1783430245082202112 |
---|---|
author | Li, Jie Tang, Danming Ireland, Stephen C. Wang, Yanzhuang |
author_facet | Li, Jie Tang, Danming Ireland, Stephen C. Wang, Yanzhuang |
author_sort | Li, Jie |
collection | PubMed |
description | In mammalian cells, the Golgi reassembly stacking protein of 65 kDa (GRASP65) has been implicated in both Golgi stacking and ribbon linking by forming trans-oligomers. To better understand its function and regulation, we used biochemical methods to identify the DnaJ homolog subfamily A member 1 (DjA1) as a novel GRASP65-binding protein. In cells, depletion of DjA1 resulted in Golgi fragmentation, short and improperly aligned cisternae, and delayed Golgi reassembly after nocodazole washout. In vitro, immunodepletion of DjA1 from interphase cytosol reduced its activity to enhance GRASP65 oligomerization and Golgi membrane fusion, while adding purified DjA1 enhanced GRASP65 oligomerization. DjA1 is a cochaperone of Heat shock cognate 71-kDa protein (Hsc70), but the activity of DjA1 in Golgi structure formation is independent of its cochaperone activity or Hsc70, rather, through DjA1-GRASP65 interaction to promote GRASP65 oligomerization. Thus, DjA1 interacts with GRASP65 to enhance Golgi structure formation through the promotion of GRASP65 trans-oligomerization. |
format | Online Article Text |
id | pubmed-6594443 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-65944432019-07-05 DjA1 maintains Golgi integrity via interaction with GRASP65 Li, Jie Tang, Danming Ireland, Stephen C. Wang, Yanzhuang Mol Biol Cell Articles In mammalian cells, the Golgi reassembly stacking protein of 65 kDa (GRASP65) has been implicated in both Golgi stacking and ribbon linking by forming trans-oligomers. To better understand its function and regulation, we used biochemical methods to identify the DnaJ homolog subfamily A member 1 (DjA1) as a novel GRASP65-binding protein. In cells, depletion of DjA1 resulted in Golgi fragmentation, short and improperly aligned cisternae, and delayed Golgi reassembly after nocodazole washout. In vitro, immunodepletion of DjA1 from interphase cytosol reduced its activity to enhance GRASP65 oligomerization and Golgi membrane fusion, while adding purified DjA1 enhanced GRASP65 oligomerization. DjA1 is a cochaperone of Heat shock cognate 71-kDa protein (Hsc70), but the activity of DjA1 in Golgi structure formation is independent of its cochaperone activity or Hsc70, rather, through DjA1-GRASP65 interaction to promote GRASP65 oligomerization. Thus, DjA1 interacts with GRASP65 to enhance Golgi structure formation through the promotion of GRASP65 trans-oligomerization. The American Society for Cell Biology 2019-02-15 /pmc/articles/PMC6594443/ /pubmed/30566031 http://dx.doi.org/10.1091/mbc.E18-10-0613 Text en © 2019 Li et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. http://creativecommons.org/licenses/by-nc-sa/3.0 This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License. |
spellingShingle | Articles Li, Jie Tang, Danming Ireland, Stephen C. Wang, Yanzhuang DjA1 maintains Golgi integrity via interaction with GRASP65 |
title | DjA1 maintains Golgi integrity via interaction with GRASP65 |
title_full | DjA1 maintains Golgi integrity via interaction with GRASP65 |
title_fullStr | DjA1 maintains Golgi integrity via interaction with GRASP65 |
title_full_unstemmed | DjA1 maintains Golgi integrity via interaction with GRASP65 |
title_short | DjA1 maintains Golgi integrity via interaction with GRASP65 |
title_sort | dja1 maintains golgi integrity via interaction with grasp65 |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6594443/ https://www.ncbi.nlm.nih.gov/pubmed/30566031 http://dx.doi.org/10.1091/mbc.E18-10-0613 |
work_keys_str_mv | AT lijie dja1maintainsgolgiintegrityviainteractionwithgrasp65 AT tangdanming dja1maintainsgolgiintegrityviainteractionwithgrasp65 AT irelandstephenc dja1maintainsgolgiintegrityviainteractionwithgrasp65 AT wangyanzhuang dja1maintainsgolgiintegrityviainteractionwithgrasp65 |