Cooperative activity of Ref-1/APE and ERp57 in reductive activation of transcription factors

Grillo, Caterina; D’Ambrosio, Chiara; Scaloni, Andrea; Maceroni, Manola; Merluzzi, Sonia; Turano, Carlo; Altieri, Fabio

doi:10.1016/j.freeradbiomed.2006.06.016

Cited by 70 publications

(73 citation statements)

References 31 publications

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“…In particular, ERp57 was found essential for the phosphorylation of histone H2AX, an indicator of genotoxic stress [70]. Interestingly, in a search of nuclear proteins interacting with purified ERp57, the latter was found in HepG2 cells to associate not only with APE/Ref-1, as mentioned before, but also with Ku80, Ku70 and nuclear matrix protein 200/hPso4 [13], all proteins involved in the process of DNA repair, so that somehow ERp57 appears to participate in more than one way in this process, albeit with a still unknown mechanism. Other ERp57-containing complexes have been described following a proteomic comparative study of paclitaxel-resistant and sensitive ovary cancer cells, where overexpressed ERp57 was identified as a major marker for chemotherapeutic resistance.…”

Section: Erp57 In the Nucleusmentioning

confidence: 52%

“…In view of its relative abundance in the cytosol, such function might indeed be important in this compartment. A definite implication of the redox properties of ERp57 has emerged from the finding of its interaction with APE/Ref-1, which is a multifunctional protein, acting not only as a reductant for a variety of transcription factors, but also as a protein involved in DNA repair and a transcription factor itself [13]. The interaction appears to take place through the a and a' domains of ERp57 [13] (Fig.…”

Section: Erp57 In the Cytosolmentioning

confidence: 99%

“…ERp57, instead, needs to associate with calreticulin, which is a lectin and therefore binds glycoproteins, so that ERp57 can in turn subject these to catalysis. However, also ERp57 has been found to interact with high affinity to a number of small ligands [11] and even macromolecules [12,13], so that other sites must be present. In some cases they have been identified in the a' and a domains (Fig.…”

Section: Introductionmentioning

confidence: 99%

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ERp57/GRP58: A protein with multiple functions

Turano

Gaucci

Grillo

et al. 2011

Cellular and Molecular Biology Letters

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114

108

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Abbreviations used: 1α,25-(OH) 2 D 3 -1α,25-dihydroxycholecalciferol and calcitriol; APE/Ref-1 -apurinic (apyrimidinic) endonuclease/redox-factor 1; CRP -C-reactive protein; ER -endoplasmic reticulum; ERAD endoplasmic reticulum associated protein degradation; mTORC -mammalian target of rapamycin complex; PDI -protein disulfide isomerase; PKC -protein kinases C; PLA 2 -phospholipases A 2 ; Plc -peptide loading complex; PLC -phospholipase C; PrP SC -scrapie prion protein (misfolded prions); STAT -signal transducer and activator of transcription; STAT3 -signal transducer and activator of transcription 3; SV40 virus -simian virus 40; VDR -vitamin D receptor Review ERp57/GRP58: A PROTEIN WITH MULTIPLE FUNCTIONSCARLO TURANO*, ELISA GAUCCI, CATERINA GRILLO and SILVIA CHICHIARELLI Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza -Università di Roma, Italy Abstract: The protein ERp57/GRP58 is a stress-responsive protein and a component of the protein disulfide isomerase family. Its functions in the endoplasmic reticulum are well known, concerning mainly the proper folding and quality control of glycoproteins, and participation in the assembly of the major histocompatibility complex class 1. However, ERp57 is present in many other subcellular locations, where it is involved in a variety of functions, primarily suggested by its participation in complexes with other proteins and even with DNA. While in some instances these roles need to be confirmed by further studies, a great number of observations support the participation of ERp57 in signal transduction from the cell surface, in regulatory processes taking place in the nucleus, and in multimeric protein complexes involved in DNA repair.

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Section: Erp57 In the Nucleusmentioning

confidence: 52%

Section: Erp57 In the Cytosolmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

ERp57/GRP58: A protein with multiple functions

Turano

Gaucci

Grillo

et al. 2011

Cellular and Molecular Biology Letters

Self Cite

114

108

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show abstract

“…Indeed, ERp57 is a widely expressed protein disulfide isomerase that regulates protein-protein interactions via a redox mechanism based on the activity of its two thioredoxin-like domains. It acts as a cellular redox sensor to adapt cells to oxidative insults (50). The redox-sensitive mechanism that depends on ERp57 expression activates mTORC1, which mediates the correct assembly of mTOR complexes (51).…”

Section: Discussionmentioning

confidence: 99%

A Transcriptome-proteome Integrated Network Identifies Endoplasmic Reticulum thiol oxidoreductase (ERp57) as a Hub that Mediates Bone Metastasis

Santana-Codina

Carretero

Sanz‐Pamplona

et al. 2013

Molecular & Cellular Proteomics

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Bone metastasis is the most common distant relapse in breast cancer. The identification of key proteins involved in the osteotropic phenotype would represent a major step toward the development of new prognostic markers and therapeutic improvements. The aim of this study was to characterize functional phenotypes that favor bone metastasis in human breast cancer. We used the human breast cancer cell line MDA-MB-231 and its osteotropic BO2 subclone to identify crucial proteins in bone metastatic growth. We identified 31 proteins, 15 underexpressed and 16 overexpressed, in BO2 cells compared with parental cells. We employed a network-modeling approach in which these 31 candidate proteins were prioritized with respect to their potential in metastasis formation, based on the topology of the protein-protein interaction network and differential expression. The protein-protein interaction network provided a framework to study the functional relationships between biological molecules by attributing functions to genes whose functions had not been characterized. The combination of expression profiles and protein interactions revealed an endoplasmic reticulum-thiol oxidoreductase, ERp57, function- Large-scale genomic analysis has provided a wealth of information on biologically relevant systems, and the ability to analyze this information is crucial to uncovering important biological relationships. In breast cancer, microarray gene expression analysis is a promising technique for providing consistent patterns of variation in bone metastasis gene expression; the most common metastasis (80%) in those women who progress to an advanced stage of disease (1-4). However, a large number of genes with many diverse functions are identified as prognostic markers, without revealing much about the underlying biological mechanism.Genes that enhance or suppress bone metastasis are associated with multiple cellular processes that normally occur during metastasis progression, including survival and proliferation in the bone marrow microenvironment, and modification of bone structure and function (1). Many genes in this group encode secretory or cell surface proteins involved in cell homing to bone, angiogenesis, invasion, and osteoclast recruitment (1, 2, 5). Moreover, emerging evidence from murine models suggests that tumor-specific endocrine factors systematically stimulate the quiescent bone marrow compartment (BM), resulting in a BM-derived tumor microenvironment From the ‡Biological Clues

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“…We have suggested that ERp57, through its disulphide isomerase activity, might have a role in the proper folding and compartmentalization of TUBB3 in response to paclitaxel treatment. Though mainly localised in the ER, ERp57 has been detected in the cytosol, where it participates to signal transduction and transcription regulation by activation of STAT3 (11) and in association with the cytoskeleton (3), and in the nucleus, where it influences the DNA binding of transcription factors or of structural nuclear proteins (49,50) and is involved in the cellular response to drug treatment (3,13,51).…”

Section: Discussionmentioning

confidence: 99%

Characterisation of a multimeric protein complex associated with ERp57 within the nucleus in paclitaxel-sensitive and -resistant epithelial ovarian cancer cells: The involvement of specific conformational states of β-actin

Cicchillitti¹,

Corte

Michele

et al. 2010

Int J Oncol

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Abstract. Ovarian cancer is the second most frequently diagnosed malignancy of the reproductive system and is the leading cause of gynecological cancer mortality. Although the majority of advanced ovarian carcinomas initially respond successfully to taxane-based chemotherapy, resistance to chemotherapy remains the primary factor accounting for the low 5-year survival in this patient population. Recent data obtained by our group demonstrate that the disulphide isomerase ERp57 is strongly modulated in paclitaxel resistance suggesting that it may represent a chemoresistance biomarker in ovarian cancer. In the present study, we characterise a nuclear multimeric complex where ERp57 is associated with protein species involved in cell division and gene expression, as Nucleolin, Nucleophosmin, Vimentin, Aurora kinase C and ß-actin. In particular, we show that the occurrence of the interaction of nuclear ERp57 with ß-actin is associated with paclitaxel resistance and that specific actin conformations modulate this complex. We propose the involvement of the nuclear ERp57 complex in mechanisms associated with chromosome segregation in which specific conformational states of actin play a role in the pathway involved in paclitaxel resistance.

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Cooperative activity of Ref-1/APE and ERp57 in reductive activation of transcription factors

Cited by 70 publications

References 31 publications

ERp57/GRP58: A protein with multiple functions

ERp57/GRP58: A protein with multiple functions

A Transcriptome-proteome Integrated Network Identifies Endoplasmic Reticulum thiol oxidoreductase (ERp57) as a Hub that Mediates Bone Metastasis

Characterisation of a multimeric protein complex associated with ERp57 within the nucleus in paclitaxel-sensitive and -resistant epithelial ovarian cancer cells: The involvement of specific conformational states of β-actin

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