https://scholars.lib.ntu.edu.tw/handle/123456789/160353
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor | 臺大醫學院-分子醫學研究所;臺大醫學院-臨床醫學研究所; | - |
dc.contributor.author | Yang, Fu-Chia | en |
dc.contributor.author | Lin, Ya-Huei | en |
dc.contributor.author | Chen, Wei-Hao | en |
dc.contributor.author | Huang, Jing-Yi | en |
dc.contributor.author | Chang, Hsin-Yun | en |
dc.contributor.author | Su, Su-Hui | en |
dc.contributor.author | Wang, Hsiao-Ting | en |
dc.contributor.author | Chiang, Chun-Yi | en |
dc.contributor.author | Hsu, Pang-Hung | en |
dc.contributor.author | Tsai, Ming-Daw | en |
dc.contributor.author | Tan, Bertrand Chin-Ming | en |
dc.contributor.author | Lee, Sheng-Chung | en |
dc.creator | Yang, Fu-Chia;Lin, Ya-Huei;Chen, Wei-Hao;Huang, Jing-Yi;Chang, Hsin-Yun;Su, Su-Hui;Wang, Hsiao-Ting;Chiang, Chun-Yi;Hsu, Pang-Hung;Tsai, Ming-Daw;Tan, Bertrand Chin-Ming;Lee, Sheng-Chung | en |
dc.creator | 呂勝春 | zh-tw |
dc.date | 2013 | - |
dc.date.accessioned | 2017-06-22T06:13:51Z | - |
dc.date.accessioned | 2018-07-09T01:26:52Z | - |
dc.date.available | 2017-06-22T06:13:51Z | - |
dc.date.available | 2018-07-09T01:26:52Z | - |
dc.date.issued | 2013 | - |
dc.identifier.uri | http://ntur.lib.ntu.edu.tw//handle/246246/279553 | - |
dc.description.abstract | Salt-inducible kinase 2 (SIK2) is an important regulator of cAMP response element-binding protein-mediated gene expression in various cell types and is the only AMP-activated protein kinase family member known to interact with the p97/valosin-containing protein (VCP) ATPase. Previously, we have demonstrated that SIK2 can regulate autophagy when proteasomal function is compromised. Here we report that physical and functional interactions between SIK2 and p97/VCP underlie the regulation of endoplasmic reticulum (ER)-associated protein degradation (ERAD). SIK2 co-localizes with p97/VCP in the ER membrane and stimulates its ATPase activity through direct phosphorylation. Although the expression of wild-type recombinant SIK2 accelerated the degradation and removal of ERAD substrates, the kinase-deficient variant conversely had no effect. Furthermore, down-regulation of endogenous SIK2 or mutation of the SIK2 target site on p97/VCP led to impaired degradation of ERAD substrates and disruption of ER homeostasis. Collectively, these findings highlight a mechanism by which the interplay between SIK2 and p97/VCP contributes to the regulation of ERAD in mammalian cells. | - |
dc.language | en-us | - |
dc.relation | J. Biol. Chem., 288(47), 33861-33872 | - |
dc.relation.ispartof | Journal of Biological Chemistry | en_US |
dc.subject | ER Stress | - |
dc.subject | ER-associated Degradation | - |
dc.subject | ERAD | - |
dc.subject | Protein Degradation | - |
dc.subject | Unfolded Protein Response | - |
dc.subject | SIK2 | - |
dc.subject | p97 | - |
dc.subject | VCP | - |
dc.title | Interaction between Salt-inducible Kinase 2 (SIK2) and p97/Valosin-containing Protein (VCP) Regulates Endoplasmic Reticulum (ER)-associated Protein Degradation in Mammalian Cells | - |
dc.identifier.doi | 10.1074/jbc.M113.492199 | - |
dc.relation.pages | 33861-33872 | - |
item.grantfulltext | none | - |
item.fulltext | no fulltext | - |
顯示於: | 分子醫學研究所 |
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