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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45544

Title: Reversible Acetylation Regulates Salt-Inducible Kinase (SIK2) and Its Function in Autophagy
Authors: Fu-Chia Yang;Bertrand Chin-Ming Tan;Wei-Hao Chen;Ya-Huei Lin;Jing-Yi Huang;Hsin-Yun Chang;Hui-Yu Sun;Pang-Hung Hsu;Gunn-Guang Liou;James Sheng;Ching-Jin Chang;Chau-Chung Han;Ming-Daw Tsai;Sheng-Chung Lee
Contributors: 國立臺灣海洋大學:生命科學系
Date: 2013
Issue Date: 2018-03-26T05:42:39Z
Publisher: The Journal of Biological Chemistry
Abstract: 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-43Δ 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.
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45544
Appears in Collections:[生命科學系] 期刊論文

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