Session 3The CREB Family: key regulators of hepatic metabolism
Références (28)
Genome Wide Analysis of CREB Target Genes Reveals A Core Promoter Requirement for cAMP Responsiveness
Mol Cell
(2003)- et al.
Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at Serine 133
Cell
(1989) Transcriptional Attenuation Following cAMP Induction Requires PP-1-Mediated Dephosphorylation of CREB
Cell
(1992)Distinct activation domains within cAMP response element-binding protein (CREB) mediate basal and cAMP-stimulated transcription
J Biol Chem
(1993)Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator-coactivator interactions
Cell
(1997)TORCs: transducers of regulated CREB activity
Mol Cell
(2003)Cyclic-AMP-responsive DNA-binding protein: structure based on a cloned placental cDNA
Science
(1988)A cluster of phosphorylation sites on the cyclic AMP-regulated nuclear factor CREB predicted by its sequence
Nature
(1989)- et al.
Tanscriptional Regulation by the Phosphorylation Dependent Factor CREB
Nature Reviews-Molecular Cell Biology
(2001) Coupling of hormonal stimulation and transcription via cyclic AMP-responsive factor CREB is rate limited by nuclear entry of protein kinase A
Mol & Cell Biol
(1993)
Nuclear Protein Phosphatase 2A Dephosphorylates Protein kinase A-Phosphorylated CREB and Regulates CREB Transcriptional Stimulation
Molecular and Cellular Biology
Attenuation of a phosphorylation-dependent activator by an HDAC-PP1 complex
Nature Structural Biology
Analysis of a PK-A Dependent Activator in CREB Reveals a New Role For the CREM Family of Repressors
Nature
Phosphorylated CREB binds specifically to the nuclear protein CBP
Nature
Cited by (36)
Lithium chloride promotes lipid accumulation through increased reactive oxygen species generation
2020, Biochimica et Biophysica Acta - Molecular and Cell Biology of LipidsCitation Excerpt :In contrast, lithium promotes CREB phosphorylation and CREB-directed gene transcription in HIT-T15 hamster pancreatic beta cells in accordance with our results [40]. CREB is implicated in both negative and positive regulation of hepatic lipid metabolism [41]. CREB appears to contribute to lipid metabolism in a complex manner due to its differential expression and functions of various CREB-regulated factors that regulate target genes in a cell- or tissue-specific manner.
CREB family: A significant role in liver fibrosis
2019, BiochimieCitation Excerpt :Traditionally, CREB family belongs to CREB/ATF family, a superfamily of basic region/leucine zipper (bZIP) transcriptional regulators [9]. CREB family is classified into CREB, CRE modulator (CREM), and activating transcription factor-1 (ATF-1) [9,10]. CREB3, CREB3L3, and et al. are often identified as CREB/ATF family members [11].
Regulation of hepatic gluconeogenesis by nuclear factor Y transcription factor in mice
2018, Journal of Biological ChemistryCitation Excerpt :PEPCK and G6Pase are the primary enzymes in the gluconeogenic pathway in the liver. It is well known that the cAMP signaling pathway plays a central role in controlling the expression of G6pc and Pck1 (25, 26). The response of NF-Y to cAMP challenge in the mouse liver suggested that this transcription factor might mediate gluoconeogenic gene expression.
Dysregulated phosphorylation and nuclear translocation of cyclic AMP response element binding protein (CREB) in rat liver after chronic ethanol binge
2012, European Journal of PharmacologyCitation Excerpt :CREB is a 43-kDa protein that belongs to the beta leucine zipper family of transcription factors. CREB is emerging as a key transcription factor regulating diverse hepatic functions (Mayr and Montminy, 2001; Montminy et al., 2004). CREB has been implicated in hepatocyte proliferation during liver regeneration induced by partial hepatectomy (Rudnick et al., 2001).
Class IIa histone deacetylases are hormone-activated regulators of FOXO and mammalian glucose homeostasis
2011, CellCitation Excerpt :We report here that phosphorylation of class IIa HDACs is controlled in liver by LKB1-dependent kinases, but in response to glucagon, class IIa HDACs are rapidly dephosphorylated and translocate to the nucleus where they associate with the G6pc and Pck1 promoters. Importantly, glucagon is known to stimulate expression of these genes in hepatocytes through PKA-mediated effects on CREB (Montminy et al., 2004) and through effects on FOXO of an unknown mechanism (Matsumoto et al., 2007). We demonstrate that class IIa HDACs recruit HDAC3 to gluconeogenic loci and regulate FOXO acetylation in hepatocytes and liver.