Role of E2F1 in endoplasmic reticulum stress signaling

Kyung Mi Park; Dong Joon Kim; Sang Gi Paik; Soo Jung Kim; Young Il Yeom

Role of E2F1 in endoplasmic reticulum stress signaling

Kyung Mi Park, Dong Joon Kim, Sang Gi Paik, Soo Jung Kim, Young Il Yeom

Research output: Contribution to journal › Article › peer-review

Abstract

The transcription factor E2F1 coordinates cell cycle progression and induces apoptosis in response to DNA damage stress. Aside from DNA damage, the role of E2F1 in the endoplasmic reticulum (ER) stress signaling pathways is unclear. We found that E2Fl^-/- murine embryonic fibroblasts (MEFs) are resistant to apoptosis triggered by the ER stress inducer thapsigargin. In addition, E2F1 deficiency results in enhanced phosphorylation of eukaryotic translation initiation factor 2α (eIF2α). These results therefore indicate that E2F1 deficiency increases phosphorylation of eIF2α in response to ER stress triggered by thapsigargin, and suggest that the reduction in ER stress-induced apoptosis. in E2F1 deficient cells is related to the high level of eIF2α phosphorylation.

Original language	English (US)
Pages (from-to)	356-359
Number of pages	4
Journal	Molecules and Cells
Volume	21
Issue number	3
State	Published - Jun 30 2006
Externally published	Yes

Keywords

E2F1
Endoplasmic reticulum stress
Eukaryotic translation initiation factor 2α (eIF2α)
Thapsigargin

ASJC Scopus subject areas

Molecular Biology
Cell Biology

Cite this

@article{198492d2e9854add8be88fbc5b172736,

title = "Role of E2F1 in endoplasmic reticulum stress signaling",

abstract = "The transcription factor E2F1 coordinates cell cycle progression and induces apoptosis in response to DNA damage stress. Aside from DNA damage, the role of E2F1 in the endoplasmic reticulum (ER) stress signaling pathways is unclear. We found that E2Fl-/- murine embryonic fibroblasts (MEFs) are resistant to apoptosis triggered by the ER stress inducer thapsigargin. In addition, E2F1 deficiency results in enhanced phosphorylation of eukaryotic translation initiation factor 2α (eIF2α). These results therefore indicate that E2F1 deficiency increases phosphorylation of eIF2α in response to ER stress triggered by thapsigargin, and suggest that the reduction in ER stress-induced apoptosis. in E2F1 deficient cells is related to the high level of eIF2α phosphorylation.",

keywords = "E2F1, Endoplasmic reticulum stress, Eukaryotic translation initiation factor 2α (eIF2α), Thapsigargin",

author = "Park, {Kyung Mi} and Kim, {Dong Joon} and Paik, {Sang Gi} and Kim, {Soo Jung} and Yeom, {Young Il}",

year = "2006",

month = jun,

day = "30",

language = "English (US)",

volume = "21",

pages = "356--359",

journal = "Molecules and Cells",

issn = "1016-8478",

publisher = "Korean Society for Molecular and Cellular Biology",

number = "3",

}

TY - JOUR

T1 - Role of E2F1 in endoplasmic reticulum stress signaling

AU - Park, Kyung Mi

AU - Kim, Dong Joon

AU - Paik, Sang Gi

AU - Kim, Soo Jung

AU - Yeom, Young Il

PY - 2006/6/30

Y1 - 2006/6/30

N2 - The transcription factor E2F1 coordinates cell cycle progression and induces apoptosis in response to DNA damage stress. Aside from DNA damage, the role of E2F1 in the endoplasmic reticulum (ER) stress signaling pathways is unclear. We found that E2Fl-/- murine embryonic fibroblasts (MEFs) are resistant to apoptosis triggered by the ER stress inducer thapsigargin. In addition, E2F1 deficiency results in enhanced phosphorylation of eukaryotic translation initiation factor 2α (eIF2α). These results therefore indicate that E2F1 deficiency increases phosphorylation of eIF2α in response to ER stress triggered by thapsigargin, and suggest that the reduction in ER stress-induced apoptosis. in E2F1 deficient cells is related to the high level of eIF2α phosphorylation.

AB - The transcription factor E2F1 coordinates cell cycle progression and induces apoptosis in response to DNA damage stress. Aside from DNA damage, the role of E2F1 in the endoplasmic reticulum (ER) stress signaling pathways is unclear. We found that E2Fl-/- murine embryonic fibroblasts (MEFs) are resistant to apoptosis triggered by the ER stress inducer thapsigargin. In addition, E2F1 deficiency results in enhanced phosphorylation of eukaryotic translation initiation factor 2α (eIF2α). These results therefore indicate that E2F1 deficiency increases phosphorylation of eIF2α in response to ER stress triggered by thapsigargin, and suggest that the reduction in ER stress-induced apoptosis. in E2F1 deficient cells is related to the high level of eIF2α phosphorylation.

KW - E2F1

KW - Endoplasmic reticulum stress

KW - Eukaryotic translation initiation factor 2α (eIF2α)

KW - Thapsigargin

UR - http://www.scopus.com/inward/record.url?scp=33745851170&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33745851170&partnerID=8YFLogxK

M3 - Article

C2 - 16819297

AN - SCOPUS:33745851170

SN - 1016-8478

VL - 21

SP - 356

EP - 359

JO - Molecules and Cells

JF - Molecules and Cells

IS - 3

ER -

Role of E2F1 in endoplasmic reticulum stress signaling

Abstract

Keywords

ASJC Scopus subject areas

Other files and links

Fingerprint

Cite this