| Item type |
文献 / Documents(1) |
| 公開日 |
2023-11-09 |
| アクセス権 |
|
|
アクセス権 |
open access |
| 資源タイプ |
|
|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
journal article |
| 出版社版DOI |
|
|
|
関連識別子 |
https://doi.org/10.1016/j.celrep.2022.111868 |
|
|
関連名称 |
10.1016/j.celrep.2022.111868 |
| 出版タイプ |
|
|
出版タイプ |
VoR |
|
出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| タイトル |
|
|
タイトル |
The Golgi-resident protein ACBD3 concentrates STING at ER-Golgi contact sites to drive export from the ER |
| 著者 |
茂谷, 康
田良島, 典子
ニシノ, コウヘイ
ヤマウチ, シュンヤ
南川, 典昭
小迫, 英尊
|
| 抄録 |
|
|
内容記述 |
STING, an endoplasmic reticulum (ER)-resident receptor for cyclic di-nucleotides (CDNs), is essential for innate immune responses. Upon CDN binding, STING moves from the ER to the Golgi, where it activates downstream type-I interferon (IFN) signaling. General cargo proteins exit from the ER via concentration at ER exit sites. However, the mechanism of STING concentration is poorly understood. Here, we visualize the ER exit sites of STING by blocking its transport at low temperature or by live-cell imaging with the cell-permeable ligand bis-pivSATE-2'F-c-di-dAMP, which we have developed. After ligand binding, STING forms punctate foci at non-canonical ER exit sites. Unbiased proteomic screens and super-resolution microscopy show that the Golgi-resident protein ACBD3/GCP60 recognizes and concentrates ligand-bound STING at specialized ER-Golgi contact sites. Depletion of ACBD3 impairs STING ER-to-Golgi trafficking and type-I IFN responses. Our results identify the ACBD3-mediated non-canonical cargo concentration system that drives the ER exit of STING. |
| 書誌情報 |
en : Cell Reports
巻 41,
号 12,
p. 111868,
発行日 2022-12-20
|
| 収録物ID |
|
|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
22111247 |
| 出版者 |
|
|
出版者 |
Elsevier |
| 権利情報 |
|
|
権利情報 |
This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
| EID |
|
|
識別子 |
396210 |
| 言語 |
|
|
言語 |
eng |
celrep_41_12_111868.pdf (5.21 MB)
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