TY - JOUR
T1 - The selenoprotein methionine sulfoxide reductase B1 (MSRB1)
AU - Tarrago, Lionel
AU - Kaya, Alaattin
AU - Kim, Hwa Young
AU - Manta, Bruno
AU - Lee, Byung Cheon
AU - Gladyshev, Vadim N.
N1 - Funding Information:
L. Tarrago's research is supported by funding from the Excellence Initiative of Aix-Marseille University – A*MIDEX, a French “Investissements d’Avenir” programme and is part of the Institute of Microbiology, Bioenergies and Biotechnology – IM2B ( AMX-19-IET-006 ), by the Novo Nordisk Foundation Grant NNF20OC0059697 and by intramural grant from the French National Research Institute for Agriculture, Food and Environment (INRAE) . Research in the Manta laboratory is supported by The Pew Charitable Trust (grant 00028662 ), Agencia Nacional de Innovacion e Investigacion-Uruguay , grant FCE_1_2021_1_166635 , and Fondo de Convergencia Estructural del Mercosur (FOCEM) grant gs14 COF 03/11. Research in the Lee laboratory is supported by National Research Foundation of Korea (NRF) grants ( 2021R1A2C4086540 ) funded by the Korean government (Ministry of Science, ICT & Future Planning) . Research in the Gladyshev laboratory is supported by NIH grants.
Publisher Copyright:
© 2022
PY - 2022/10
Y1 - 2022/10
N2 - Methionine (Met) can be oxidized to methionine sulfoxide (MetO), which exist as R- and S-diastereomers. Present in all three domains of life, methionine sulfoxide reductases (MSR) are the enzymes that reduce MetO back to Met. Most characterized among them are MSRA and MSRB, which are strictly stereospecific for the S- and R-diastereomers of MetO, respectively. While the majority of MSRs use a catalytic Cys to reduce their substrates, some employ selenocysteine. This is the case of mammalian MSRB1, which was initially discovered as selenoprotein SELR or SELX and later was found to exhibit an MSRB activity. Genomic analyses demonstrated its occurrence in most animal lineages, and biochemical and structural analyses uncovered its catalytic mechanism. The use of transgenic mice and mammalian cell culture revealed its physiological importance in the protection against oxidative stress, maintenance of neuronal cells, cognition, cancer cell proliferation, and the immune response. Coincident with the discovery of Met oxidizing MICAL enzymes, recent findings of MSRB1 regulating the innate immunity response through reversible stereospecific Met-R-oxidation of cytoskeletal actin opened up new avenues for biological importance of MSRB1 and its role in disease. In this review, we discuss the current state of research on MSRB1, compare it with other animal Msrs, and offer a perspective on further understanding of biological functions of this selenoprotein.
AB - Methionine (Met) can be oxidized to methionine sulfoxide (MetO), which exist as R- and S-diastereomers. Present in all three domains of life, methionine sulfoxide reductases (MSR) are the enzymes that reduce MetO back to Met. Most characterized among them are MSRA and MSRB, which are strictly stereospecific for the S- and R-diastereomers of MetO, respectively. While the majority of MSRs use a catalytic Cys to reduce their substrates, some employ selenocysteine. This is the case of mammalian MSRB1, which was initially discovered as selenoprotein SELR or SELX and later was found to exhibit an MSRB activity. Genomic analyses demonstrated its occurrence in most animal lineages, and biochemical and structural analyses uncovered its catalytic mechanism. The use of transgenic mice and mammalian cell culture revealed its physiological importance in the protection against oxidative stress, maintenance of neuronal cells, cognition, cancer cell proliferation, and the immune response. Coincident with the discovery of Met oxidizing MICAL enzymes, recent findings of MSRB1 regulating the innate immunity response through reversible stereospecific Met-R-oxidation of cytoskeletal actin opened up new avenues for biological importance of MSRB1 and its role in disease. In this review, we discuss the current state of research on MSRB1, compare it with other animal Msrs, and offer a perspective on further understanding of biological functions of this selenoprotein.
KW - Methionine sulfoxide
KW - Methionine sulfoxide reductase
KW - Oxidative stress
KW - Protein oxidation
KW - Redox signaling
KW - Selenium
KW - Selenoprotein
UR - http://www.scopus.com/inward/record.url?scp=85138099809&partnerID=8YFLogxK
U2 - 10.1016/j.freeradbiomed.2022.08.043
DO - 10.1016/j.freeradbiomed.2022.08.043
M3 - Review article
C2 - 36084791
AN - SCOPUS:85138099809
SN - 0891-5849
VL - 191
SP - 228
EP - 240
JO - Free Radical Biology and Medicine
JF - Free Radical Biology and Medicine
ER -