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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Salt-inducible kinase 2

Top mentioned proteins: CREB, AMPK, Insulin, MSK, mTORC2
Papers on SIK2
Practical Experience of the Application of a Weighted Burden Test to Whole Exome Sequence Data for Obesity and Schizophrenia.
UK10K Consortium et al., London, United Kingdom. In Ann Hum Genet, Jan 2016
The diverse oncogenic and tumor suppressor roles of salt-inducible kinase (SIK) in cancer.
Pei et al., Xuzhou, China. In Expert Opin Ther Targets, Dec 2015
Overexpression of SIK2 and SIK3 is discovered in many tumors.
Salt-inducible Kinase 3 Signaling Is Important for the Gluconeogenic Programs in Mouse Hepatocytes.
Takemori et al., Ōsaka, Japan. In J Biol Chem, Aug 2015
These results suggest that SIK3, rather than SIK1, SIK2, or AMPKs, acts as the predominant suppressor in gluconeogenic gene expression in the hepatocytes.
Salt-inducible kinase 3 deficiency exacerbates lipopolysaccharide-induced endotoxin shock accompanied by increased levels of pro-inflammatory molecules in mice.
Takemori et al., Ibaraki, Japan. In Immunology, Jun 2015
LPS injection (10 mg/kg) led to the death of all SIK3-knockout (KO) mice within 48 hr after treatment, whereas only one mouse died in the SIK1-KO (n = 8), SIK2-KO (n = 9) and wild-type (n = 8 or 9) groups.
Salt-inducible kinase 2 regulates mitotic progression and transcription in prostate cancer.
Mills et al., Cambridge, United Kingdom. In Mol Cancer Res, Apr 2015
UNLABELLED: Salt-inducible kinase 2 (SIK2) is a multifunctional kinase of the AMPK family that plays a role in CREB1-mediated gene transcription and was recently reported to have therapeutic potential in ovarian cancer.
The association between Salt-inducible kinase 2 (SIK2) and gamma isoform of the regulatory subunit B55 of PP2A (B55gamma) contributes to the survival of glioma cells under glucose depletion through inhibiting the phosphorylation of S6K.
Liu et al., Shanghai, China. In Cancer Cell Int, 2014
From proteomic analysis, we found B55gamma binds with and up regulates SIK2 through the stabilization of SIK2 protein which is required for the B55gamma-mediated suppression of S6K pathway.
Injury-induced immune responses in Hydra.
Galliot et al., Genève, Switzerland. In Semin Immunol, 2014
These regulations point to an enhanced cytoprotection via ROS signaling (Nrf, C/EBP, p62/SQSMT1-l2), TNFR and TLR signaling (TNFR16-like, TRAF2l, TRAF5l, jun, fos-related, SIK2, ATF1/CREB, LRRC28, LRRC40, LRRK2), proteasomal activity (p62/SQSMT1-l1, Ced6/Gulf, NEDD8-conjugating enzyme Ubc12), stress proteins (CRYAB1, CRYAB2, HSP16.2,
SIK2 regulates insulin secretion.
Stoffel et al., Zürich, Switzerland. In Nat Cell Biol, 2014
The AMPK-related kinase SIK2 (salt-inducible kinase 2) is now shown to be stabilized in pancreatic β-cells following glucose stimulation, leading to improved systemic glucose homeostasis by regulating cellular calcium flux and insulin secretion.
Role of the SIK2-p35-PJA2 complex in pancreatic β-cell functional compensation.
Screaton et al., In Nat Cell Biol, 2014
Here we delineate a complex consisting of the AMPK-related kinase SIK2, the CDK5 activator CDK5R1 (also known as p35) and the E3 ligase PJA2 essential for β-cell functional compensation.
The regulation and function of the NUAK family.
Zhao et al., Taipei, Taiwan. In J Mol Endocrinol, 2013
Twelve AMPK-related kinases (ARKs; BRSK1, BRSK2, NUAK1, NUAK2, QIK, QSK, SIK, MARK1, MARK2, MARK3, MARK4, and MELK) have been identified recently.
Regulation of insulin sensitivity by serine/threonine phosphorylation of insulin receptor substrate proteins IRS1 and IRS2.
White et al., Boston, United States. In Diabetologia, 2012
In cultured cells, insulin-stimulated kinases (including atypical PKC, AKT, SIK2, mTOR, S6K1, ERK1/2 and ROCK1) mediate feedback (autologous) S/T phosphorylation of IRS, with both positive and negative effects on insulin sensitivity.
Mapping the hallmarks of lung adenocarcinoma with massively parallel sequencing.
Meyerson et al., Cambridge, United States. In Cell, 2012
Whole-genome sequence analysis revealed frequent structural rearrangements, including in-frame exonic alterations within EGFR and SIK2 kinases.
The AMPK-related kinase SIK2 is regulated by cAMP via phosphorylation at Ser358 in adipocytes.
Göransson et al., Lund, Sweden. In Biochem J, 2012
In adipocytes, Ser358 (not Ser587) is the main site phosphorylated and responsible for the binding of SIK2 to 14-3-3 proteins.
Inositol-1,4,5-trisphosphate receptor regulates hepatic gluconeogenesis in fasting and diabetes.
Montminy et al., Los Angeles, United States. In Nature, 2012
Glucagon promotes CRTC2 dephosphorylation in part through the protein kinase A (PKA)-mediated inhibition of the CRTC2 kinase SIK2.
SIK2 is a key regulator for neuronal survival after ischemia via TORC1-CREB.
Kitagawa et al., Suita, Japan. In Neuron, 2011
These findings suggest that SIK2 plays critical roles in neuronal survival, is modulated by CaMK I/IV, and regulates CREB via TORC1.
Downregulation of SIK2 expression promotes the melanogenic program in mice.
Takemori et al., Ibaraki, Japan. In Pigment Cell Melanoma Res, 2010
SIK2 represses eumelanogenesis in mice.
Salt-inducible kinase 2 links transcriptional coactivator p300 phosphorylation to the prevention of ChREBP-dependent hepatic steatosis in mice.
Dentin et al., Paris, France. In J Clin Invest, 2010
low SIK2 activity was associated with increased p300 HAT activity, ChREBP hyperacetylation, and hepatic steatosis
SIK2 is a centrosome kinase required for bipolar mitotic spindle formation that provides a potential target for therapy in ovarian cancer.
Bast et al., Houston, United States. In Cancer Cell, 2010
Depletion of SIK2 also delayed G1/S transition and reduced AKT phosphorylation. Higher expression of SIK2 significantly correlated with poor survival in patients with high-grade serous ovarian cancers
The regulation and function of mammalian AMPK-related kinases.
Carling et al., London, United Kingdom. In Acta Physiol (oxf), 2009
Recently, 12 AMPK-related kinases (BRSK1, BRSK2, NUAK1, NUAK2, QIK, QSK, SIK, MARK1, MARK2, MARK3, MARK4 and MELK) were identified that are closely related by sequence homology to the catalytic domain of AMPK.
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