Methionine sulfoxide reductase B3 protects from endoplasmic reticulum stress in Drosophila and in mammalian cells

Geun Hee Kwak; Do Hwan Lim; Jee Yun Han; Young Sik Lee; Hwa Young Kim

doi:10.1016/j.bbrc.2012.02.128

Methionine sulfoxide reductase B3 protects from endoplasmic reticulum stress in Drosophila and in mammalian cells

Geun Hee Kwak, Do Hwan Lim, Jee Yun Han, Young Sik Lee, Hwa Young Kim

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

13 Citations (Scopus)

Abstract

Methionine sulfoxide reductase B3A (MsrB3A), which catalyzes the stereospecific reduction of methionine-R-sulfoxide to methionine, is localized to the endoplasmic reticulum (ER). Here, we report a critical role of the ER-targeted MsrB3 in protection against ER stress in Drosophila and in mammalian cells. Flies overexpressing human MsrB3A exhibited significantly increased resistance to ER stress induced by dithiothreitol. These flies also showed slightly enhanced resistance to tunicamycin-induced ER stress. In addition, overexpression of MsrB3A in mammalian cells increased resistance to dithiothreitol- and thapsigargin-induced ER stresses. However, MsrB3A overexpression had no effect on the resistance to tunicamycin-induced ER stress. Knockdown of MsrB3A in mammalian cells led to a significant decrease in the resistance to thapsigargin-induced ER stress, but had no effects on the resistance to either dithiothreitol- or tunicamycin-induced ER stress. Collectively, our data provide evidence that the ER-type of MsrB3 plays an important role in protection against ER stress, suggesting that MsrB3 may be involved in the regulation of ER homeostasis.

Original language	English
Pages (from-to)	130-135
Number of pages	6
Journal	Biochemical and biophysical research communications
Volume	420
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2012.02.128
Publication status	Published - 2012 Mar 30

Bibliographical note

Funding Information:
This work was supported by the National Research Foundation of Korea Grants 2010-0001240 and 2010-0020596 (to H.-Y.K.), and by Mid-career Researcher Program through NRF grant funded by the MEST ( 2011-0016863 to Y.S.L.). D.H.L. was supported by Hi Seoul Science/Humanities Fellowship from Seoul Scholarship Foundation.

Copyright:
Copyright 2012 Elsevier B.V., All rights reserved.

Keywords

ER homeostasis
ER stress
Methionine sulfoxide reductase
MsrB
Unfolded protein response

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2012.02.128

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title = "Methionine sulfoxide reductase B3 protects from endoplasmic reticulum stress in Drosophila and in mammalian cells",

abstract = "Methionine sulfoxide reductase B3A (MsrB3A), which catalyzes the stereospecific reduction of methionine-R-sulfoxide to methionine, is localized to the endoplasmic reticulum (ER). Here, we report a critical role of the ER-targeted MsrB3 in protection against ER stress in Drosophila and in mammalian cells. Flies overexpressing human MsrB3A exhibited significantly increased resistance to ER stress induced by dithiothreitol. These flies also showed slightly enhanced resistance to tunicamycin-induced ER stress. In addition, overexpression of MsrB3A in mammalian cells increased resistance to dithiothreitol- and thapsigargin-induced ER stresses. However, MsrB3A overexpression had no effect on the resistance to tunicamycin-induced ER stress. Knockdown of MsrB3A in mammalian cells led to a significant decrease in the resistance to thapsigargin-induced ER stress, but had no effects on the resistance to either dithiothreitol- or tunicamycin-induced ER stress. Collectively, our data provide evidence that the ER-type of MsrB3 plays an important role in protection against ER stress, suggesting that MsrB3 may be involved in the regulation of ER homeostasis.",

keywords = "ER homeostasis, ER stress, Methionine sulfoxide reductase, MsrB, Unfolded protein response",

author = "Kwak, {Geun Hee} and Lim, {Do Hwan} and Han, {Jee Yun} and Lee, {Young Sik} and Kim, {Hwa Young}",

note = "Funding Information: This work was supported by the National Research Foundation of Korea Grants 2010-0001240 and 2010-0020596 (to H.-Y.K.), and by Mid-career Researcher Program through NRF grant funded by the MEST ( 2011-0016863 to Y.S.L.). D.H.L. was supported by Hi Seoul Science/Humanities Fellowship from Seoul Scholarship Foundation. Copyright: Copyright 2012 Elsevier B.V., All rights reserved.",

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AU - Kwak, Geun Hee

AU - Lim, Do Hwan

AU - Han, Jee Yun

AU - Lee, Young Sik

AU - Kim, Hwa Young

N1 - Funding Information: This work was supported by the National Research Foundation of Korea Grants 2010-0001240 and 2010-0020596 (to H.-Y.K.), and by Mid-career Researcher Program through NRF grant funded by the MEST ( 2011-0016863 to Y.S.L.). D.H.L. was supported by Hi Seoul Science/Humanities Fellowship from Seoul Scholarship Foundation. Copyright: Copyright 2012 Elsevier B.V., All rights reserved.

PY - 2012/3/30

Y1 - 2012/3/30

N2 - Methionine sulfoxide reductase B3A (MsrB3A), which catalyzes the stereospecific reduction of methionine-R-sulfoxide to methionine, is localized to the endoplasmic reticulum (ER). Here, we report a critical role of the ER-targeted MsrB3 in protection against ER stress in Drosophila and in mammalian cells. Flies overexpressing human MsrB3A exhibited significantly increased resistance to ER stress induced by dithiothreitol. These flies also showed slightly enhanced resistance to tunicamycin-induced ER stress. In addition, overexpression of MsrB3A in mammalian cells increased resistance to dithiothreitol- and thapsigargin-induced ER stresses. However, MsrB3A overexpression had no effect on the resistance to tunicamycin-induced ER stress. Knockdown of MsrB3A in mammalian cells led to a significant decrease in the resistance to thapsigargin-induced ER stress, but had no effects on the resistance to either dithiothreitol- or tunicamycin-induced ER stress. Collectively, our data provide evidence that the ER-type of MsrB3 plays an important role in protection against ER stress, suggesting that MsrB3 may be involved in the regulation of ER homeostasis.

AB - Methionine sulfoxide reductase B3A (MsrB3A), which catalyzes the stereospecific reduction of methionine-R-sulfoxide to methionine, is localized to the endoplasmic reticulum (ER). Here, we report a critical role of the ER-targeted MsrB3 in protection against ER stress in Drosophila and in mammalian cells. Flies overexpressing human MsrB3A exhibited significantly increased resistance to ER stress induced by dithiothreitol. These flies also showed slightly enhanced resistance to tunicamycin-induced ER stress. In addition, overexpression of MsrB3A in mammalian cells increased resistance to dithiothreitol- and thapsigargin-induced ER stresses. However, MsrB3A overexpression had no effect on the resistance to tunicamycin-induced ER stress. Knockdown of MsrB3A in mammalian cells led to a significant decrease in the resistance to thapsigargin-induced ER stress, but had no effects on the resistance to either dithiothreitol- or tunicamycin-induced ER stress. Collectively, our data provide evidence that the ER-type of MsrB3 plays an important role in protection against ER stress, suggesting that MsrB3 may be involved in the regulation of ER homeostasis.

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KW - Methionine sulfoxide reductase

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KW - Unfolded protein response

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Methionine sulfoxide reductase B3 protects from endoplasmic reticulum stress in Drosophila and in mammalian cells

Abstract

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Keywords

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