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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45540

Title: Interaction between salt-inducible kinase 2 (SIK2) and p97/valosin-containing protein (VCP) regulates endoplasmic reticulum (ER)-associated protein degradation in mammalian cells
Authors: Fu-Chia Yang;Ya-Huei Lin;Wei-Hao Chen;Jing-Yi Huang;Hsin-Yun Chang;Su-Hui Su;Hsiao-Ting Wang;Chun-Yi Chiang;Pang-Hung Hsu;Ming-Daw Tsai;Bertrand Chin-Ming Tan;Sheng-Chung Lee
Contributors: 國立臺灣海洋大學:生命科學系
Date: 2013
Issue Date: 2018-03-26T01:33:46Z
Publisher: The Journal of Biological Chemistry
Abstract: 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.
Relation: 288
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45540
Appears in Collections:[生命科學系] 期刊論文

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