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

28 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 (US)
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 - Jan 11 2013
Externally published	Yes

Bibliographical note

Funding Information:
We thank K.H. Bae for critical reading of manuscript. This work was supported by KRIBB and research grants from the National Research Foundation of Korea (NRF) ( PSC0011112 and 2011-0008842 ) and National Project for Personalized Genomic Medicine, Ministry for Health & Welfare, Republic of Korea ( A111218-CP03 ).

Keywords

AGR2
Dimerization
ER stress
UPR signaling pathway

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.bbrc.2012.11.105

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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}",

note = "Funding Information: We thank K.H. Bae for critical reading of manuscript. This work was supported by KRIBB and research grants from the National Research Foundation of Korea (NRF) ( PSC0011112 and 2011-0008842 ) and National Project for Personalized Genomic Medicine, Ministry for Health & Welfare, Republic of Korea ( A111218-CP03 ).",

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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

N1 - Funding Information: We thank K.H. Bae for critical reading of manuscript. This work was supported by KRIBB and research grants from the National Research Foundation of Korea (NRF) ( PSC0011112 and 2011-0008842 ) and National Project for Personalized Genomic Medicine, Ministry for Health & Welfare, Republic of Korea ( A111218-CP03 ).

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

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

Abstract

Bibliographical note

Keywords

UN SDGs

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