https://scholars.lib.ntu.edu.tw/handle/123456789/160285
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor | 臺大醫學院-口腔生物科學研究所;臺大醫學院-分子醫學研究所; | - |
dc.contributor.author | Lee, Chia-Wei | en |
dc.contributor.author | Yang, Fu-Chia | en |
dc.contributor.author | Chang, Hsin-Yun | en |
dc.contributor.author | HAN-YI E. CHOU | en |
dc.contributor.author | Tan, Bertrand Chin-Ming | en |
dc.contributor.author | Lee, Sheng-Chung | en |
dc.creator | Lee, Chia-Wei;Yang, Fu-Chia;Chang, Hsin-Yun;Chou, Hanyi;Tan, Bertrand Chin-Ming;Lee, Sheng-Chung | en |
dc.creator | 周涵怡;呂勝春 | zh-tw |
dc.date | 2014 | - |
dc.date.accessioned | 2017-05-25T07:29:38Z | - |
dc.date.accessioned | 2018-07-09T01:23:56Z | - |
dc.date.available | 2017-05-25T07:29:38Z | - |
dc.date.available | 2018-07-09T01:23:56Z | - |
dc.date.issued | 2014 | - |
dc.identifier.uri | http://ntur.lib.ntu.edu.tw//handle/246246/278982 | - |
dc.description.abstract | Salt-inducible kinase 2 (SIK2) is the only AMP-activated kinase (AMPK) family member known to interact with protein phosphatase 2 (PP2A). However, the functional aspects of this complex are largely unknown. Here we report that the SIK2 center dot PP2A complex preserves both kinase and phosphatase activities. In this capacity, SIK2 attenuates the association of the PP2A repressor, the protein phosphatase methylesterase-1 (PME-1), thus preserving the methylation status of the PP2A catalytic subunit. Furthermore, the SIK2 center dot PP2A holoenzyme complex dephosphorylates and inactivates Ca2+/calmodulin-dependent protein kinase I (CaMKI), an upstream kinase for phosphorylating PME-1/Ser(15). The functionally antagonistic SIK2 center dot PP2A and CaMKI and PME-1 networks thus constitute a negative feedback loop that modulates the phosphatase activity of PP2A. Depletion of SIK2 led to disruption of the SIK2 center dot PP2A complex, activation of CaMKI, and downstream effects, including phosphorylation of HDAC5/Ser259, sequestration of HDAC5 in the cytoplasm, and activation of myocyte-specific enhancer factor 2C (MEF2C)-mediated gene expression. These results suggest that the SIK2 center dot PP2A complex functions in the regulation of MEF2C-dependent transcription. Furthermore, this study suggests that the tightly linked regulatory loop comprised of the SIK2 center dot PP2A and CaMKI and PME-1 networks may function in fine-tuning cell proliferation and stress response. | - |
dc.language | en-us | - |
dc.relation | J. Biol. Chem., 289(30), 21108-21119 | - |
dc.relation.ispartof | Journal of Biological Chemistry | en_US |
dc.title | Interaction between Salt-inducible Kinase 2 and Protein Phosphatase 2A Regulates the Activity of Calcium/Calmodulin-dependent Protein Kinase I and Protein Phosphatase Methylesterase-1 | - |
dc.identifier.doi | 10.1074/jbc.M113.540229 | - |
dc.relation.pages | 21108-21119 | - |
item.grantfulltext | none | - |
item.fulltext | no fulltext | - |
crisitem.author.dept | Biochemical Science and Technology | - |
crisitem.author.dept | School of Dentistry | - |
crisitem.author.dept | Oral Biology | - |
crisitem.author.orcid | 0000-0002-8925-7421 | - |
crisitem.author.parentorg | College of Life Science | - |
crisitem.author.parentorg | College of Medicine | - |
crisitem.author.parentorg | College of Medicine | - |
顯示於: | 分子醫學研究所 |
在 IR 系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。