Search: onr:"swepub:oai:lup.lub.lu.se:1e0aab87-e13a-47c4-b51b-13a4009f4a5f" > The LKB1-salt-induc...
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000 | 03530naa a2200541 4500 | |
001 | oai:lup.lub.lu.se:1e0aab87-e13a-47c4-b51b-13a4009f4a5f | |
003 | SwePub | |
008 | 160401s2014 | |||||||||||000 ||eng| | |
024 | 7 | a https://lup.lub.lu.se/record/46156222 URI |
024 | 7 | a https://doi.org/10.1038/ncomms55352 DOI |
040 | a (SwePub)lu | |
041 | a engb eng | |
042 | 9 SwePub | |
072 | 7 | a art2 swepub-publicationtype |
072 | 7 | a ref2 swepub-contenttype |
100 | 1 | a Patel, Kashyap4 aut |
245 | 1 0 | a The LKB1-salt-inducible kinase pathway functions as a key gluconeogenic suppressor in the liver. |
264 | c 2014-08-04 | |
264 | 1 | b Springer Science and Business Media LLC,c 2014 |
338 | a electronic2 rdacarrier | |
520 | a LKB1 is a master kinase that regulates metabolism and growth through adenosine monophosphate-activated protein kinase (AMPK) and 12 other closely related kinases. Liver-specific ablation of LKB1 causes increased glucose production in hepatocytes in vitro and hyperglycaemia in fasting mice in vivo. Here we report that the salt-inducible kinases (SIK1, 2 and 3), members of the AMPK-related kinase family, play a key role as gluconeogenic suppressors downstream of LKB1 in the liver. The selective SIK inhibitor HG-9-91-01 promotes dephosphorylation of transcriptional co-activators CRTC2/3 resulting in enhanced gluconeogenic gene expression and glucose production in hepatocytes, an effect that is abolished when an HG-9-91-01-insensitive mutant SIK is introduced or LKB1 is ablated. Although SIK2 was proposed as a key regulator of insulin-mediated suppression of gluconeogenesis, we provide genetic evidence that liver-specific ablation of SIK2 alone has no effect on gluconeogenesis and insulin does not modulate SIK2 phosphorylation or activity. Collectively, we demonstrate that the LKB1-SIK pathway functions as a key gluconeogenic gatekeeper in the liver. | |
650 | 7 | a MEDICIN OCH HÄLSOVETENSKAPx Klinisk medicinx Endokrinologi och diabetes0 (SwePub)302052 hsv//swe |
650 | 7 | a MEDICAL AND HEALTH SCIENCESx Clinical Medicinex Endocrinology and Diabetes0 (SwePub)302052 hsv//eng |
700 | 1 | a Foretz, Marc4 aut |
700 | 1 | a Marion, Allison4 aut |
700 | 1 | a Campbell, David G4 aut |
700 | 1 | a Gourlay, Robert4 aut |
700 | 1 | a Boudaba, Nadia4 aut |
700 | 1 | a Tournier, Emilie4 aut |
700 | 1 | a Titchenell, Paul4 aut |
700 | 1 | a Peggie, Mark4 aut |
700 | 1 | a Deak, Maria4 aut |
700 | 1 | a Wan, Min4 aut |
700 | 1 | a Kaestner, Klaus H4 aut |
700 | 1 | a Göransson, Olgau Lund University,Lunds universitet,Proteinfosforylering,Forskargrupper vid Lunds universitet,Protein Phosphorylation,Lund University Research Groups4 aut0 (Swepub:lu)medk-ogo |
700 | 1 | a Viollet, Benoit4 aut |
700 | 1 | a Gray, Nathanael S4 aut |
700 | 1 | a Birnbaum, Morris J4 aut |
700 | 1 | a Sutherland, Calum4 aut |
700 | 1 | a Sakamoto, Kei4 aut |
710 | 2 | a Proteinfosforyleringb Forskargrupper vid Lunds universitet4 org |
773 | 0 | t Nature Communicationsd : Springer Science and Business Media LLCg 5:Aug 4q 5:Aug 4x 2041-1723 |
856 | 4 | u https://portal.research.lu.se/files/4288635/7864277x primaryx freey FULLTEXT |
856 | 4 | u http://www.ncbi.nlm.nih.gov/pubmed/25088745?dopt=Abstractx freey FULLTEXT |
856 | 4 | u http://dx.doi.org/10.1038/ncomms5535x freey FULLTEXT |
856 | 4 | u https://www.nature.com/articles/ncomms5535.pdf |
856 | 4 8 | u https://lup.lub.lu.se/record/4615622 |
856 | 4 8 | u https://doi.org/10.1038/ncomms5535 |
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