https://scholars.lib.ntu.edu.tw/handle/123456789/160352
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 | Tan, Bertrand Chin-Ming | en |
dc.contributor.author | Chen, Wei-Hao | en |
dc.contributor.author | Lin, Ya-Huei | en |
dc.contributor.author | Huang, Jing-Yi | en |
dc.contributor.author | Chang, Hsin-Yun | en |
dc.contributor.author | Sun, Hui-Yu | en |
dc.contributor.author | Hsu, Pang-Hung | en |
dc.contributor.author | Liou, Gunn-Guang | en |
dc.contributor.author | Shen, James | en |
dc.contributor.author | Chang, Ching-Jin | en |
dc.contributor.author | Han, Chau-Chung | en |
dc.contributor.author | Tsai, Ming-Daw | en |
dc.contributor.author | Lee, Sheng-Chung | en |
dc.creator | Yang, Fu-Chia;Tan, Bertrand Chin-Ming;Chen, Wei-Hao;Lin, Ya-Huei;Huang, Jing-Yi;Chang, Hsin-Yun;Sun, Hui-Yu;Hsu, Pang-Hung;Liou, Gunn-Guang;Shen, James;Chang, Ching-Jin;Han, Chau-Chung;Tsai, Ming-Daw;Lee, Sheng-Chung | en |
dc.creator | 呂勝春 | zh-tw |
dc.date | 2013 | - |
dc.date.accessioned | 2017-06-22T06:01:40Z | - |
dc.date.accessioned | 2018-07-09T01:26:51Z | - |
dc.date.available | 2017-06-22T06:01:40Z | - |
dc.date.available | 2018-07-09T01:26:51Z | - |
dc.date.issued | 2013 | - |
dc.identifier.uri | http://ntur.lib.ntu.edu.tw//handle/246246/279524 | - |
dc.description.abstract | Salt-inducible kinase 2 (SIK2) is a serine/threonine protein kinase belonging to the AMP-activated protein kinase (AMPK) family. SIK2 has been shown to function in the insulin-signaling pathway during adipocyte differentiation and to modulate CREB-mediated gene expression in response to hormones and nutrients. However, molecular mechanisms underlying the regulation of SIK2 kinase activity remains largely elusive. Here we report a dynamic, post-translational regulation of its kinase activity that is coordinated by an acetylation-deaceytlation switch, p300/CBP-mediated Lys-53 acetylation inhibits SIK2 kinase activity, whereas HDAC6-mediated deacetylation restores the activity. Interestingly, overexpression of acetylation-mimetic mutant of SIK2 (SIK2-K53Q), but not the nonacetylatable K53R variant, resulted in accumulation of autophagosomes. Further consistent with a role in autophagy, knockdown of SIK2 abrogated autophagosome and lysosome fusion. Consequently, SIK2 and its kinase activity are indispensable for the removal of TDP-43 Delta inclusion bodies. Our findings uncover SIK2 as a critical determinant in autophagy progression and further suggest a mechanism in which the interplay among kinase and deacetylase activities contributes to cellular protein pool homeostasis. | - |
dc.language | en-us | - |
dc.relation | J. Biol. Chem., 288(9), 6227-6237 | - |
dc.relation.ispartof | Journal of Biological Chemistry | en_US |
dc.title | Reversible Acetylation Regulates Salt-inducible Kinase (SIK2) and Its Function in Autophagy | - |
dc.identifier.doi | 10.1074/jbc.M112.431239 | - |
dc.relation.pages | 6227-6237 | - |
item.grantfulltext | none | - |
item.fulltext | no fulltext | - |
顯示於: | 分子醫學研究所 |
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