Dimerization of pro-oncogenic protein Anterior Gradient 2 is required for the interaction with BiP/GRP78

Joohyun Ryu; Sung Goo Park; Phil Young Lee; Sayeon Cho; Do Hee Lee; Gwang Hoon Kim; Jeong Hoon Kim; Byoung Chul Park

doi:10.1016/j.bbrc.2012.11.105

Dimerization of pro-oncogenic protein Anterior Gradient 2 is required for the interaction with BiP/GRP78

Joohyun Ryu, Sung Goo Park, Phil Young Lee, Sayeon Cho, Do Hee Lee, Gwang Hoon Kim, Jeong Hoon Kim, Byoung Chul Park

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

29 Scopus citations

Abstract

Anterior Gradient 2 (AGR2), an ER stress-inducible protein, has been reported to be localized in endoplasmic reticulum (ER) and its level is elevated in numerous metastatic cancers. Recently, it has been demonstrated that AGR2 is involved in the control of ER homeostasis. However, the molecular mechanism how AGR2 regulates ER stress response remains unclear. Herein we show that AGR2 homo-dimerizes through an intermolecular disulfide bond. Moreover, dimerization of AGR2 attenuates ER stress-induced cell death through the association with BiP/GRP78. Thus, these results suggest that dimerization of AGR2 is crucial in mediating the ER stress signaling pathway.

Original language	English
Pages (from-to)	610-615
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	430
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2012.11.105
State	Published - 11 Jan 2013
Externally published	Yes

Keywords

AGR2
Dimerization
ER stress
UPR signaling pathway

Access to Document

10.1016/j.bbrc.2012.11.105

Cite this

@article{99007cb1ebb240dab6dbd0571ec034f6,

title = "Dimerization of pro-oncogenic protein Anterior Gradient 2 is required for the interaction with BiP/GRP78",

abstract = "Anterior Gradient 2 (AGR2), an ER stress-inducible protein, has been reported to be localized in endoplasmic reticulum (ER) and its level is elevated in numerous metastatic cancers. Recently, it has been demonstrated that AGR2 is involved in the control of ER homeostasis. However, the molecular mechanism how AGR2 regulates ER stress response remains unclear. Herein we show that AGR2 homo-dimerizes through an intermolecular disulfide bond. Moreover, dimerization of AGR2 attenuates ER stress-induced cell death through the association with BiP/GRP78. Thus, these results suggest that dimerization of AGR2 is crucial in mediating the ER stress signaling pathway.",

keywords = "AGR2, Dimerization, ER stress, UPR signaling pathway",

author = "Joohyun Ryu and Park, {Sung Goo} and Lee, {Phil Young} and Sayeon Cho and Lee, {Do Hee} and Kim, {Gwang Hoon} and Kim, {Jeong Hoon} and Park, {Byoung Chul}",

year = "2013",

month = jan,

day = "11",

doi = "10.1016/j.bbrc.2012.11.105",

language = "English",

volume = "430",

pages = "610--615",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier B.V.",

number = "2",

}

TY - JOUR

T1 - Dimerization of pro-oncogenic protein Anterior Gradient 2 is required for the interaction with BiP/GRP78

AU - Ryu, Joohyun

AU - Park, Sung Goo

AU - Lee, Phil Young

AU - Cho, Sayeon

AU - Lee, Do Hee

AU - Kim, Gwang Hoon

AU - Kim, Jeong Hoon

AU - Park, Byoung Chul

PY - 2013/1/11

Y1 - 2013/1/11

N2 - Anterior Gradient 2 (AGR2), an ER stress-inducible protein, has been reported to be localized in endoplasmic reticulum (ER) and its level is elevated in numerous metastatic cancers. Recently, it has been demonstrated that AGR2 is involved in the control of ER homeostasis. However, the molecular mechanism how AGR2 regulates ER stress response remains unclear. Herein we show that AGR2 homo-dimerizes through an intermolecular disulfide bond. Moreover, dimerization of AGR2 attenuates ER stress-induced cell death through the association with BiP/GRP78. Thus, these results suggest that dimerization of AGR2 is crucial in mediating the ER stress signaling pathway.

AB - Anterior Gradient 2 (AGR2), an ER stress-inducible protein, has been reported to be localized in endoplasmic reticulum (ER) and its level is elevated in numerous metastatic cancers. Recently, it has been demonstrated that AGR2 is involved in the control of ER homeostasis. However, the molecular mechanism how AGR2 regulates ER stress response remains unclear. Herein we show that AGR2 homo-dimerizes through an intermolecular disulfide bond. Moreover, dimerization of AGR2 attenuates ER stress-induced cell death through the association with BiP/GRP78. Thus, these results suggest that dimerization of AGR2 is crucial in mediating the ER stress signaling pathway.

KW - AGR2

KW - Dimerization

KW - ER stress

KW - UPR signaling pathway

UR - http://www.scopus.com/inward/record.url?scp=84872316957&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2012.11.105

DO - 10.1016/j.bbrc.2012.11.105

M3 - Article

C2 - 23220234

AN - SCOPUS:84872316957

SN - 0006-291X

VL - 430

SP - 610

EP - 615

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

Dimerization of pro-oncogenic protein Anterior Gradient 2 is required for the interaction with BiP/GRP78

Abstract

Keywords

Access to Document

Fingerprint

Cite this