Calcium Ionophore A23187 Induces Expression of Glucose-Regulated Genes and Their Heterologous Fusion Genes

Resendez, E; Attenello, J W; Grafsky, A; Chang, Chung-Ming; Lee, A S

doi:10.1128/mcb.5.6.1212-1219.1985

Molecular and Cellular Biology

1985

DOI: 10.1128/mcb.5.6.1212-1219.1985

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Calcium Ionophore A23187 Induces Expression of Glucose-Regulated Genes and Their Heterologous Fusion Genes

E Resendez¹,

J W Attenello²,

A Grafsky³

et al.

Abstract: Using two cDNA clones which encode hamster genes specifically induced by glucose starvation, we demonstrated that an 8- and 30-fold increase, respectively, in the transcription rates of these genes was coordinately effected by calcium ionophore A23187 treatment, resulting in a similar increase in the steady-state levels of their mRNAs. This response was observed within several hours of ionophore treatment in several mammalian cell types and appeared to be specifically mediated by A23187 but not by other ionoph… Show more

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Cited by 6 publications

References 20 publications

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Endoplasmic Reticulum Chaperones Are Involved in the Morphogenesis of Rotavirus Infectious Particles

Maruri-Avidal

López

2008

J Virol

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The final assembly of rotavirus particles takes place in the endoplasmic reticulum (ER). In this work, we evaluated by RNA interference the relevance to rotavirus assembly and infectivity of grp78, protein disulfide isomerase (PDI), grp94, calnexin, calreticulin, and ERp57, members of the two ER folding systems described herein. Silencing the expression of grp94 and Erp57 had no effect on rotavirus infectivity, while knocking down the expression of any of the other four chaperons caused a reduction in the yield of infectious virus of about 50%. In grp78-silenced cells, the maturation of the oligosaccharide chains of NSP4 was retarded. In cells with reduced levels of calnexin, the oxidative folding of VP7 was impaired and the trimming of NSP4 was accelerated, and in calreticulin-silenced cells, the formation of disulfide bonds of VP7 was also accelerated. The knockdown of PDI impaired the formation and/or rearrangement of the VP7 disulfide bonds. All these conditions also affected the correct assembly of virus particles, since compared with virions from control cells, they showed an altered susceptibility to EGTA and heat treatments, a decreased specific infectivity, and a diminished reactivity to VP7 with monoclonal antibody M60, which recognizes only this protein when its disulfide bonds have been correctly formed. In the case of grp78-silenced cells, the virus produced bound less efficiently to MA104 cells than virus obtained from control cells. All these results suggest that these chaperones are involved in the quality control of rotavirus morphogenesis. The complexity of the steps of rotavirus assembly that occur in the ER provide a useful model for studying the organization and operation of the complex network of chaperones involved in maintaining the quality control of this organelle.

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Endoplasmic Reticulum Chaperones Are Involved in the Morphogenesis of Rotavirus Infectious Particles

Maruri-Avidal

López

2008

J Virol

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BiP (GRP78) and Endoplasmin (GRP94) Are Induced following Rotavirus Infection and Bind Transiently to an Endoplasmic Reticulum-Localized Virion Component

Bellamy

Taylor

1998

J Virol

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Rotavirus infection induces profound alterations in the morphology and biochemistry of the host cell. Using two-dimensional (2D) gel electrophoresis combined with metabolic labeling, we have identified four proteins that are specifically upregulated in rotavirus-infected cells. Two of these have been identified as BiP (GRP78) and endoplasmin (GRP94), members of a family of glucose-regulated chaperone proteins that reside in the endoplasmic reticulum (ER) lumen, the site of rotavirus morphogenesis. The level of mRNA and the transcriptional activity of the BiP and endoplasmin genes are increased markedly in rotavirus-infected cells, and these genes are also induced when a single rotavirus protein, the nonstructural glycoprotein NSP4, is expressed in MA104 cells. However, NSP4 does not associate with either BiP or endoplasmin, implying that the mechanism of BiP and endoplasmin gene activation by NSP4 may differ from that triggered by viral membrane glycoproteins of other viruses. The interaction of BiP and endoplasmin with rotavirus structural polypeptides suggests that these chaperones are involved in the process of viral maturation in the ER lumen.

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Transactivation of the grp78 Promoter by Malfolded Proteins, Glycosylation Block, and Calcium Ionophore Is Mediated through a Proximal Region Containing a CCAAT Motif Which Interacts with CTF/NF-I

Wooden

Navarro

et al. 1991

Molecular and Cellular Biology

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The 78-kDa glucose-regulated protein (GRP78) is a major endoplasmic reticulum (ER) protein that can form stable associations with a variety of proteins retained in the ER because of underglycosylation or other conformational changes. In this study, we provide evidence at the transcriptional level that a conformationally abnormal protein, an altered herpes simplex virus type 1 envelope protein that is retained in the ER of a mammalian cell line, transactivates the grp78 promoter. In contrast, the normal viral envelope glycoprotein does not elevate grp78 promoter activity. Using a series of 5' deletions, linker-scanning, and internal deletion mutations spanning a 100-bp region from -179 to -80, we correlate the cis-acting regulatory elements mediating the activation of grp78 by malfolded proteins, glycosylation block, and the calcium ionophore A23187. We show that they all act through the same control elements, suggesting that they share a common signal. We report here that the highly conserved grp element, while important for basal level and induced grp78 expression, is functionally redundant. The single most important element, by linker-scanning analysis, is a 10-bp region that contains a CCAAT motif. It alone is not sufficient for promoter activity, but a 40-bp region (-129 to -90) that contains this motif is essential for mediating basal level and stress inducibility of the grp78 promoter. We show that the transcription factor CTF/NF-I is able to transactivate the grp78 promoter through interaction with this CCAAT motif.

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Calcium Ionophore A23187 Induces Expression of Glucose-Regulated Genes and Their Heterologous Fusion Genes

Cited by 6 publications

References 20 publications

Endoplasmic Reticulum Chaperones Are Involved in the Morphogenesis of Rotavirus Infectious Particles

Endoplasmic Reticulum Chaperones Are Involved in the Morphogenesis of Rotavirus Infectious Particles

BiP (GRP78) and Endoplasmin (GRP94) Are Induced following Rotavirus Infection and Bind Transiently to an Endoplasmic Reticulum-Localized Virion Component

Transactivation of the grp78 Promoter by Malfolded Proteins, Glycosylation Block, and Calcium Ionophore Is Mediated through a Proximal Region Containing a CCAAT Motif Which Interacts with CTF/NF-I

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