ERC-55, a Binding Protein for the Papilloma Virus E6 Oncoprotein, Specifically Interacts with Vitamin D Receptor among Nuclear Receptors

Imai, Takeshi; Matsuda, Koichiro; Shimojima, Tukasa; Hashimoto, Takamichi; Masuhiro, Yoshikazu; Kitamoto, Takuya; Sugita, Atsuko; Suzuki, Kaori; Matsumoto, Hiroki; Masushige, S; Nogi, Yasuhisa; Muramatsu, Masami; Handa, Hiroshi; Kato, Shigeaki

doi:10.1006/bbrc.1997.6531

Biochemical and Biophysical Research Communications

1997

DOI: 10.1006/bbrc.1997.6531

|View full text |Cite

ERC-55, a Binding Protein for the Papilloma Virus E6 Oncoprotein, Specifically Interacts with Vitamin D Receptor among Nuclear Receptors

Takeshi Imai

Koichiro Matsuda

Tukasa Shimojima

et al.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

1999

2009

Publication Types

Select...

Article9

Relationship

Self Cite1

Independent8

Authors

Journals

Cited by 36 publications

(28 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Expression of a truncated form of p53 that forms inactive tetramers with endogenous wildtype p53 shortened the G2 delay in IMR-90 ®broblasts, but not as e ectively as did HPV-E6 . HPV-E6 can bind to the ERC-55 calcium binding protein, the human homologue of the Drosophila tumor suppressor discs-large, and a putative GTPase-activating protein E6TP1 (Chen et al, 1995;Gao et al, 1999;Imai et al, 1997;Kiyono et al, 1997). The di erent observations made with HPV-E6 and the truncated form of p53 suggests that other targets of HPV-E6 may contribute to the G2 checkpoint.…”

mentioning

confidence: 99%

Regulation of the G2/M transition by p53

Taylor¹,

Stark²

2001

Oncogene

1,404

1,110

View full text Add to dashboard Cite

mentioning

confidence: 99%

Regulation of the G2/M transition by p53

Taylor¹,

Stark²

2001

Oncogene

1,404

1,110

View full text Add to dashboard Cite

“…Indeed, it is reported that ERC55 interacts with the vitamin D receptor (Imai et al 1997) and the transforming oncoprotein, E6, from papillomavirus (Chen et al 1995). Research on the interaction between RCN and other proteins including other RCN family proteins is important to understand the role in malignant transformation.…”

mentioning

confidence: 99%

Distribution and Variable Expression of Secretory Pathway Protein Reticulocalbin in Normal Human Organs and Non-neoplastic Pathological Conditions

Fukuda

Oyamada

Isshiki

et al. 2006

J Histochem Cytochem.

View full text Add to dashboard Cite

Reticulocalbin (RCN) is one member of the Ca2+-binding proteins in the secretory pathway and is localized in the endoplasmic reticulum. RCN may play a role in the normal behavior and life of cells, although its detailed role remains unknown. Overexpression of RCN may also play a role in tumorigenesis, tumor invasion, and drug resistance. The new antibody for human RCN is used in the distribution of RCN in normal human organs of fetuses and adults with or without inflammation. Immunohistochemical examination demonstrated a broad distribution of RCN in various organs of fetuses and adults, predominantly in the endocrine and exocrine organs. However, RCN expression was heterogeneous in each constituent cell of some organs. Among non-epithelial organs, vascular endothelial cells, testicular germ cells, neurons, and follicular dendritic cells showed strong staining. Plasma cells were the only RCN-positive cells among hematopoietic and lymphoid cells. In inflammatory conditions, RCN expression was enhanced in both epithelial and non-epithelial cells. Heterogeneous expression of RCN indicates that the amount of RCN needed for cell behavior and life may be variable, depending on each cell type and, therefore, RCN may be helpful in establishing the cell origin of neoplasms in some organs. However, further study is needed to establish the significance of RCN in tumorigenesis and in some peculiar features of neoplasms.

show abstract

“…Overexpression of p53 in fibroblasts also causes arrest in G2 Stewart et al, 1995), and inactivation of p53 by human papillomavirus (HPV)-E6 attenuates the G2 delay that normally occurs in response to ionizing radiation (Thompson et al, 1997). However, the ability of HPV-E6 to bind to other cellular proteins (Chen et al, 1995;Imai et al, 1997;Kiyono et al, 1997;Gao et al, 1999) limits the interpretation of these findings. A truncated form of p53 that can inhibit endogenous p53 blocked DNA Figure 9.…”

mentioning

confidence: 99%

Mechanisms of G2 Arrest in Response to Overexpression of p53

Taylor

DePrimo

Agarwal

et al. 1999

MBoC

168

149

View full text Add to dashboard Cite

Overexpression of p53 causes G2 arrest, attributable in part to the loss of CDC2 activity. Transcription of cdc2 and cyclin B1, determined using reporter constructs driven by the two promoters, was suppressed in response to the induction of p53. Suppression requires the regions Ϫ287 to Ϫ123 of the cyclin B1 promoter and Ϫ104 to Ϫ74 of the cdc2 promoter. p53 did not affect the inhibitory phosphorylations of CDC2 at threonine 14 or tyrosine 15 or the activity of the cyclin-dependent kinase that activates CDC2 by phosphorylating it at threonine 161. Overexpression of p53 may also interfere with the accumulation of CDC2/cyclin B1 in the nucleus, required for cells to enter mitosis. Constitutive expression of cyclin B1, alone or in combination with the constitutively active CDC2 protein T14A Y15F, did not reverse p53-dependent G2 arrest. However, targeting cyclin B1 to the nucleus in cells also expressing CDC2 T14A Y15F did overcome this arrest. It is likely that several distinct pathways contribute to p53-dependent G2 arrest. INTRODUCTIONThe p53 tumor suppressor helps to protect mammals from developing neoplasia by blocking cell cycle progression or by inducing cell death in response to stress Levine, 1997;Agarwal et al., 1998b). p53-mediated arrest at the G1-S boundary prevents the replication of DNA damaged by ionizing or UV radiation or by chemical mutagens (Kastan et al., 1991;Gujuluva et al., 1994;Ceraline et al., 1998). G1 arrest depends on the ability of p53 to activate the transcription of specific genes (Dulic et al., 1994;Pietenpol et al., 1994). An important target, p21/waf1, inhibits cyclin-dependent kinases (CDKs) 1 2, 4, and 6, which are required to enter S phase (El-Deiry et al., 1993;Harper et al., 1993;Xiong et al., 1993). p53 also inhibits S-phase entry in response to damage to the mitotic spindle, preventing the rereplication of DNA (Cross et al., 1995), possibly by a transcription-independent mechanism (Notterman et al., 1998). p53 mediates G1 arrest in response to nucleotide deprivation, preventing DNA synthesis under conditions that would generate damaged DNA (Chernova et al., 1995;Linke et al., 1996). p53 also protects cells arrested within S phase by a lack of pyrimidine nucleotides, preventing the replication from unbalanced pools of deoxynucleoside triphosphates and consequent DNA damage (Agarwal et al., 1998a). A variety of stimuli that trigger p53-dependent cellular responses increase the ability of p53 to bind to DNA and induce the accumulation of the protein, attributable in large part to an increase in its stability (Maltzman and Czyzyk, 1984;Fritsche et al., 1993;Hupp et al., 1995). Responses to p53 vary in different types of cells and depend on the level of p53 expression. For example, thymocytes undergo p53-dependent apoptosis more readily than do fibroblasts (Lowe et al., 1993;Di Leonardo et al., 1994). In some cells, high levels of p53 induce apoptosis, whereas lower levels induce cell cycle arrest (Chen et al., 1996).p53 plays an important role in regulating the G2-M transition. ...

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

ERC-55, a Binding Protein for the Papilloma Virus E6 Oncoprotein, Specifically Interacts with Vitamin D Receptor among Nuclear Receptors

Cited by 36 publications

References 21 publications

Regulation of the G2/M transition by p53

Regulation of the G2/M transition by p53

Distribution and Variable Expression of Secretory Pathway Protein Reticulocalbin in Normal Human Organs and Non-neoplastic Pathological Conditions

Mechanisms of G2 Arrest in Response to Overexpression of p53

Contact Info

Product

Resources

About