Molecular cloning and characterization of a novel human cAMP response element-binding (CREB) gene (CREB4)

Cao, Gentao; Ni, Xiaohua; Jiang, Min; Ma, Yangyang; Cheng, Haipeng; Guo, Li; Ji, Chaoneng; Gu, Shaohua; Xie, Yi; Mao, Yumin

doi:10.1007/s100380200053

Cited by 36 publications

(35 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several downstream targets of Akt have been recognized to be apoptosis-regulatory molecules, including Bcl-2 family member Bad (24) and CREB (6). We therefore examined whether resveratrol could regulate Bad and CREB expression.…”

Section: Discussionmentioning

confidence: 99%

Pharmacological preconditioning with resveratrol: role of CREB-dependent Bcl-2 signaling via adenosine A₃ receptor activation

Das

Cordis

Maulik

et al. 2005

American Journal of Physiology-Heart and Circulatory Physiology

120

View full text Add to dashboard Cite

Recent studies demonstrated that resveratrol, a grape-derived polyphenolic phytoalexin, provides pharmacological preconditioning (PC) of the heart through a NO-dependent mechanism. Because adenosine receptors play a role in PC, we examined whether they play any role in resveratrol PC. Rats were randomly assigned to groups perfused for 15 min with 1) Krebs-Henseleit bicarbonate buffer (KHB) only; 2) KHB containing 10 μM resveratrol; 3) 10 μM resveratrol + 1 μM 8-cyclopentyl-1,3-dimethylxanthine (CPT; adenosine A1 receptor blocker); 4) 10 μM resveratrol + 1 μM 8-(3-chlorostyryl)caffeine (CSC; adenosine A2a receptor blocker); 5) 10 μM resveratrol + 1 μM 3-ethyl-5-benzyl-2-methyl-4-phenylethynyl-6-phenyl-1,4-(±)-dihydropyridine-3,5-dicarboxylate (MRS-1191; adenosine A3 receptor blocker); or 6) 10 μM resveratrol + 3 μM 2-(4-morpholinyl)-8-phenyl-1(4H)-benzopyran-4-one hydrochloride [LY-294002, phosphatidylinositol (PI)3-kinase inhibitor], and groups perfused with adenosine receptor blockers alone. Hearts were then subjected to 30-min ischemia followed by 2-h reperfusion. The results demonstrated significant cardioprotection with resveratrol evidenced by improved ventricular recovery and reduced infarct size and cardiomyocyte apoptosis. CPT and MRS 1191, but not CSC, abrogated the cardioprotective abilities of resveratrol, suggesting a role of adenosine A1 and A3 receptors in resveratrol PC. Resveratrol induced expression of Bcl-2 and caused its phosphorylation along with phosphorylation of cAMP response element-binding protein (CREB), Akt, and Bad. CPT blocked phosphorylation of Akt and Bad without affecting CREB, whereas MRS 1191 blocked phosphorylation of all compounds, including CREB. LY-294002 partially blocked the cardioprotective abilities of resveratrol. The results indicate that resveratrol preconditions the heart through activation of adenosine A1 and A3 receptors, the former transmitting a survival signal through PI3-kinase-Akt-Bcl-2 signaling pathway and the latter protecting the heart through a CREB-dependent Bcl-2 pathway in addition to an Akt-Bcl-2 pathway.

show abstract

Section: Discussionmentioning

confidence: 99%

Pharmacological preconditioning with resveratrol: role of CREB-dependent Bcl-2 signaling via adenosine A₃ receptor activation

Das

Cordis

Maulik

et al. 2005

American Journal of Physiology-Heart and Circulatory Physiology

120

View full text Add to dashboard Cite

show abstract

“…Activation of these elements can lead to induction of chaperones, translational attenuation, ER-associated degradation (ERAD) of accumulated proteins, and ultimately cell death by apoptosis (reviewed in Bernales et al 2006;Tabas and Ron 2011;Schroder 2008;Malhotra and Kaufman 2007;Mori 2009). Recently, a family of highly similar basic region leucine zipper (bZIP) proteins exemplified by CREB3/Luman (Liang et al 2006;Raggo et al 2002;Lu et al 1997;Freiman and Herr 1997) has also been implicated in the UPR in specific cell types, including CREB3L1 (Chin et al 2005;Omori et al 2001), CREB3L2 (Storlazzi et al 2003), CREB3L3 (Honma et al 1999), and CREB3L4 (Cao et al 2002;Stirling and O'Hare 2006;Qi et al 2002;Stelzer and Don 2002;Nagamori et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Herpes simplex virus-1 disarms the unfolded protein response in the early stages of infection

Burnett

Audas

Liang

et al. 2012

Cell Stress and Chaperones

View full text Add to dashboard Cite

Accumulation of mis-and unfolded proteins during viral replication can cause stress in the endoplasmic reticulum (ER) and trigger the unfolded protein response (UPR). If unchecked, this process may induce cellular changes detrimental to viral replication. In the report, we investigated the impact of HSV-1 on the UPR during lytic replication. We found that HSV-1 effectively disarms the UPR in early stages of viral infection. Only ATF6 activation was detected during early infection, but with no upregulation of target chaperone proteins. Activity of the eIF2α/ATF4 signaling arm increased at the final stage of HSV-1 replication, which may indicate completion of virion assembly and egress, thus releasing suppression of the UPR. We also found that the promoter of viral ICP0 was responsive to ER stress, an apparent mimicry of cellular UPR genes. These results suggest that HSV-1 may use ICP0 as a sensor to modulate the cellular stress response.

show abstract

“…All CREB3 family members appear to play a role in the UPR. Currently, there are four known family members in addition to Luman, including CREB-H/CREB3-like 1 (CREB3L1) (8,58), BBF2H7/CREB3L2 (73), OASIS/CREB3L3 (24), and CREB4/AIbZIP/Atce1/Tisp40/ CREB3L4 (7,53,61,71,72). Besides the well-conserved bZIP region, they all share one unique structural motif-a hydrophobic ER-transmembrane domain C-terminal to the bZIP region.…”

mentioning

confidence: 99%

A Novel Protein, Luman/CREB3 Reruitment Factor, Inhibits Luman Activation of the Unfolded Protein Response

Audas

Liang

et al. 2008

Molecular and Cellular Biology

View full text Add to dashboard Cite

Luman/CREB3 (also called LZIP) is an endoplasmic reticulum (ER)-bound cellular transcription factor. It has been implicated in the mammalian unfolded protein response (UPR), as well as herpes simplex virus reactivation from latency in sensory neurons. Here, we report the identification of a novel Luman recruitment factor (LRF). Like Luman, LRF is a UPR-responsive basic-region leucine zipper protein that is prone to proteasomal degradation. Being a highly unstable protein, LRF interacts with Luman through the leucine zipper region and promotes Luman degradation. LRF was found to recruit the nuclear form of Luman to discrete nuclear foci, which overlap with the nuclear receptor coactivator GRIP1 bodies, and repress the transactivation activity of Luman. Compared to LRF ؉/؉ mouse embryonic fibroblast (MEF) cells, the levels of CHOP, EDEM, and Herp were elevated in LRF ؊/؊ MEF cells. We propose that LRF is a negative regulator of the UPR. For Luman, it may represent another level of regulation following Luman proteolytic cleavage on the ER and nuclear translocation. In addition to inducing rapid Luman turnover, LRF may repress the transactivation potential of Luman by sequestering it in the LRF nuclear bodies away from key cofactors (such as HCF-1) that are required for transcriptional activation.The endoplasmic reticulum (ER) stress response (or unfolded protein response [UPR]) is a series of well-orchestrated cellular events to restore homeostasis in the perturbed ER. During the UPR, ER-resident molecular chaperones and foldases are induced, and translation is attenuated to reduce the load on the ER (reviewed in references 2, 49, 51, 67, 84, and 88). Unfolded proteins can also be targeted by ubiquitination for degradation by the proteasome, which is termed ER-associated degradation (ERAD) (35,60,70). Apoptosis occurs when all of these remedies have failed (16,48,63,64). Current studies of the UPR mechanism in mammalian cells have identified three signaling arms represented by three ER membrane-bound proteins, PERK (PKR-like ER kinase) (14-18), ATF6␣/␤ (19,20,75,76,92,93), and IRE1 (6,39,78,91). The activation of PERK by ER stress leads to global translational repression but selective activation of ATF4, whose downstream targets include metabolic genes and apoptosis-related CHOP (14,26,41,55,66,80). ATF6 is an ER membranebound basic-region leucine zipper (bZIP) transcription factor that is activated by the regulated intramembrane proteolysis (RIP) mechanism (5). When ATF6 cleavage is triggered by ER stress (23,87,92,93), the N terminus that encodes the transcription activation domain and the bZIP region translocates to the nucleus to activate downstream genes, such as ER chaperone BiP/GRP78 and GRP94, through the ER stress response element (ERSE) (65,68,82,89,92,93). Activated IRE1 initiates spliceosome-independent alternative splicing of XBP1u mRNA, resulting in a potent bZIP transcription factor XBP1s (6,39,59,69,91). Like ATF6, XBP1s activates ER chaperone genes via an ERSE (91), but it also activates transcript...

show abstract

Molecular cloning and characterization of a novel human cAMP response element-binding (CREB) gene (CREB4)

Cited by 36 publications

References 4 publications

Pharmacological preconditioning with resveratrol: role of CREB-dependent Bcl-2 signaling via adenosine A₃ receptor activation

Pharmacological preconditioning with resveratrol: role of CREB-dependent Bcl-2 signaling via adenosine A₃ receptor activation

Herpes simplex virus-1 disarms the unfolded protein response in the early stages of infection

A Novel Protein, Luman/CREB3 Reruitment Factor, Inhibits Luman Activation of the Unfolded Protein Response

Contact Info

Product

Resources

About

Molecular cloning and characterization of a novel human cAMP response element-binding (CREB) gene (CREB4)

Cited by 36 publications

References 4 publications

Pharmacological preconditioning with resveratrol: role of CREB-dependent Bcl-2 signaling via adenosine A3 receptor activation

Pharmacological preconditioning with resveratrol: role of CREB-dependent Bcl-2 signaling via adenosine A3 receptor activation

Herpes simplex virus-1 disarms the unfolded protein response in the early stages of infection

A Novel Protein, Luman/CREB3 Reruitment Factor, Inhibits Luman Activation of the Unfolded Protein Response

Contact Info

Product

Resources

About

Pharmacological preconditioning with resveratrol: role of CREB-dependent Bcl-2 signaling via adenosine A₃ receptor activation

Pharmacological preconditioning with resveratrol: role of CREB-dependent Bcl-2 signaling via adenosine A₃ receptor activation