The activated Notch1 receptor cooperates with α-enolase and MBP-1 in modulating c-myc activity

Kai Wen Hsu, Rong-Hong Hsieh, Yan Hwa Wu Lee, Chi Hong Chao, Kou Juey Wu, Min Jen Tseng, Tian-Shun Tsai

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

The Notch signal pathway plays multifaceted roles to promote or suppress tumorigenesis. The Notch1 receptor intracellular domain (N1IC), the activated form of the Notch1 receptor, activates the c-myc protooncogene. The complex of N1IC and transcription factor YY1 binds to the human c-myc promoter to enhance c-myc expression in a CBF1-independent manner. Here we demonstrated that N1IC interacted with the c-Myc-regulating proteins α-enolase and c-myc promoter binding protein 1 (MBP-1). Both α-enolase and MBP-1 suppressed the NUC-enhanced activity of the c-myc promoter in a CBF1-independent manner. The YY1 response element in front of the P2 c-myc promoter was essential and sufficient for the modulation of c-myc by N1IC and α-enolase or MBP-1. Furthermore, N1IC, YY1, and α-enolase or MBP-1 but not CBF1 bound to the c-myc promoter through associating with the YY1 response element. Hemin-induced erythroid differentiation was suppressed by N1IC in K562 cells. This suppression was relieved by the expression of α-enolase and MBP-1. In addition, both α-enolase and MBP-1 suppressed the N1IC-enhanced colony-forming ability through c-myc. These results indicate that the activated Notch1 receptor and α-enolase or MBP-1 cooperate in controlling c-myc expression through binding the YY1 response element of the c-myc promoter to regulate tumorigenesis.

Original languageEnglish
Pages (from-to)4829-4842
Number of pages14
JournalMolecular and Cellular Biology
Volume28
Issue number15
DOIs
Publication statusPublished - Aug 2008

Fingerprint

Notch1 Receptor
Phosphopyruvate Hydratase
Carrier Proteins
Response Elements
YY1 Transcription Factor
Carcinogenesis
Proto-Oncogene Proteins c-myc
Hemin
K562 Cells
Signal Transduction

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

The activated Notch1 receptor cooperates with α-enolase and MBP-1 in modulating c-myc activity. / Hsu, Kai Wen; Hsieh, Rong-Hong; Lee, Yan Hwa Wu; Chao, Chi Hong; Wu, Kou Juey; Tseng, Min Jen; Tsai, Tian-Shun.

In: Molecular and Cellular Biology, Vol. 28, No. 15, 08.2008, p. 4829-4842.

Research output: Contribution to journalArticle

Hsu, Kai Wen ; Hsieh, Rong-Hong ; Lee, Yan Hwa Wu ; Chao, Chi Hong ; Wu, Kou Juey ; Tseng, Min Jen ; Tsai, Tian-Shun. / The activated Notch1 receptor cooperates with α-enolase and MBP-1 in modulating c-myc activity. In: Molecular and Cellular Biology. 2008 ; Vol. 28, No. 15. pp. 4829-4842.
@article{9cedc48982354fb7aeda4d44aeadf531,
title = "The activated Notch1 receptor cooperates with α-enolase and MBP-1 in modulating c-myc activity",
abstract = "The Notch signal pathway plays multifaceted roles to promote or suppress tumorigenesis. The Notch1 receptor intracellular domain (N1IC), the activated form of the Notch1 receptor, activates the c-myc protooncogene. The complex of N1IC and transcription factor YY1 binds to the human c-myc promoter to enhance c-myc expression in a CBF1-independent manner. Here we demonstrated that N1IC interacted with the c-Myc-regulating proteins α-enolase and c-myc promoter binding protein 1 (MBP-1). Both α-enolase and MBP-1 suppressed the NUC-enhanced activity of the c-myc promoter in a CBF1-independent manner. The YY1 response element in front of the P2 c-myc promoter was essential and sufficient for the modulation of c-myc by N1IC and α-enolase or MBP-1. Furthermore, N1IC, YY1, and α-enolase or MBP-1 but not CBF1 bound to the c-myc promoter through associating with the YY1 response element. Hemin-induced erythroid differentiation was suppressed by N1IC in K562 cells. This suppression was relieved by the expression of α-enolase and MBP-1. In addition, both α-enolase and MBP-1 suppressed the N1IC-enhanced colony-forming ability through c-myc. These results indicate that the activated Notch1 receptor and α-enolase or MBP-1 cooperate in controlling c-myc expression through binding the YY1 response element of the c-myc promoter to regulate tumorigenesis.",
author = "Hsu, {Kai Wen} and Rong-Hong Hsieh and Lee, {Yan Hwa Wu} and Chao, {Chi Hong} and Wu, {Kou Juey} and Tseng, {Min Jen} and Tian-Shun Tsai",
year = "2008",
month = "8",
doi = "10.1128/MCB.00175-08",
language = "English",
volume = "28",
pages = "4829--4842",
journal = "Molecular and Cellular Biology",
issn = "0270-7306",
publisher = "American Society for Microbiology",
number = "15",

}

TY - JOUR

T1 - The activated Notch1 receptor cooperates with α-enolase and MBP-1 in modulating c-myc activity

AU - Hsu, Kai Wen

AU - Hsieh, Rong-Hong

AU - Lee, Yan Hwa Wu

AU - Chao, Chi Hong

AU - Wu, Kou Juey

AU - Tseng, Min Jen

AU - Tsai, Tian-Shun

PY - 2008/8

Y1 - 2008/8

N2 - The Notch signal pathway plays multifaceted roles to promote or suppress tumorigenesis. The Notch1 receptor intracellular domain (N1IC), the activated form of the Notch1 receptor, activates the c-myc protooncogene. The complex of N1IC and transcription factor YY1 binds to the human c-myc promoter to enhance c-myc expression in a CBF1-independent manner. Here we demonstrated that N1IC interacted with the c-Myc-regulating proteins α-enolase and c-myc promoter binding protein 1 (MBP-1). Both α-enolase and MBP-1 suppressed the NUC-enhanced activity of the c-myc promoter in a CBF1-independent manner. The YY1 response element in front of the P2 c-myc promoter was essential and sufficient for the modulation of c-myc by N1IC and α-enolase or MBP-1. Furthermore, N1IC, YY1, and α-enolase or MBP-1 but not CBF1 bound to the c-myc promoter through associating with the YY1 response element. Hemin-induced erythroid differentiation was suppressed by N1IC in K562 cells. This suppression was relieved by the expression of α-enolase and MBP-1. In addition, both α-enolase and MBP-1 suppressed the N1IC-enhanced colony-forming ability through c-myc. These results indicate that the activated Notch1 receptor and α-enolase or MBP-1 cooperate in controlling c-myc expression through binding the YY1 response element of the c-myc promoter to regulate tumorigenesis.

AB - The Notch signal pathway plays multifaceted roles to promote or suppress tumorigenesis. The Notch1 receptor intracellular domain (N1IC), the activated form of the Notch1 receptor, activates the c-myc protooncogene. The complex of N1IC and transcription factor YY1 binds to the human c-myc promoter to enhance c-myc expression in a CBF1-independent manner. Here we demonstrated that N1IC interacted with the c-Myc-regulating proteins α-enolase and c-myc promoter binding protein 1 (MBP-1). Both α-enolase and MBP-1 suppressed the NUC-enhanced activity of the c-myc promoter in a CBF1-independent manner. The YY1 response element in front of the P2 c-myc promoter was essential and sufficient for the modulation of c-myc by N1IC and α-enolase or MBP-1. Furthermore, N1IC, YY1, and α-enolase or MBP-1 but not CBF1 bound to the c-myc promoter through associating with the YY1 response element. Hemin-induced erythroid differentiation was suppressed by N1IC in K562 cells. This suppression was relieved by the expression of α-enolase and MBP-1. In addition, both α-enolase and MBP-1 suppressed the N1IC-enhanced colony-forming ability through c-myc. These results indicate that the activated Notch1 receptor and α-enolase or MBP-1 cooperate in controlling c-myc expression through binding the YY1 response element of the c-myc promoter to regulate tumorigenesis.

UR - http://www.scopus.com/inward/record.url?scp=47949083496&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=47949083496&partnerID=8YFLogxK

U2 - 10.1128/MCB.00175-08

DO - 10.1128/MCB.00175-08

M3 - Article

VL - 28

SP - 4829

EP - 4842

JO - Molecular and Cellular Biology

JF - Molecular and Cellular Biology

SN - 0270-7306

IS - 15

ER -