Regulation of protein function by reversible methionine oxidation and the role of selenoprotein MsrB1
Protein structure and function can be regulated via post-translational modifications by numerous enzymatic and nonenzymatic mechanisms. Regulation involving oxidation of sulfur-containing residues emerged as a key mechanism of redox control. Unraveling the participants and principles of such regulat...
Uložené v:
| Vydané v: | Antioxidants & redox signaling Ročník 23; číslo 10; s. 814 |
|---|---|
| Hlavní autori: | , , |
| Médium: | Journal Article |
| Jazyk: | English |
| Vydavateľské údaje: |
United States
01.10.2015
|
| Predmet: | |
| ISSN: | 1557-7716, 1557-7716 |
| On-line prístup: | Zistit podrobnosti o prístupe |
| Tagy: |
Pridať tag
Žiadne tagy, Buďte prvý, kto otaguje tento záznam!
|
| Abstract | Protein structure and function can be regulated via post-translational modifications by numerous enzymatic and nonenzymatic mechanisms. Regulation involving oxidation of sulfur-containing residues emerged as a key mechanism of redox control. Unraveling the participants and principles of such regulation is necessary for understanding the biological significance of redox control of cellular processes.
Reversible oxidation of methionine residues by monooxygenases of the Mical family and subsequent reduction of methionine sulfoxides by a selenocysteine-containing methionine sulfoxide reductase B1 (MsrB1) was found to control the assembly and disassembly of actin in mammals, and the Mical/MsrB pair similarly regulates actin in fruit flies. This finding has opened up new avenues for understanding the use of stereospecific methionine oxidation in regulating cellular processes and the roles of MsrB1 and Micals in regulation of actin dynamics.
So far, Micals have been the only known partners of MsrB1, and actin is the only target. It is important to identify additional substrates of Micals and characterize other Mical-like enzymes.
Oxidation of methionine, reviewed here, is an emerging but not well-established mechanism. Studies suggest that methionine oxidation is a form of oxidative damage of proteins, a modification that alters protein structure or function, a tool in redox signaling, and a mechanism that controls protein function. Understanding the functional impact of reversible oxidation of methionine will require identification of targets, substrates, and regulators of Micals and Msrs. Linking the biological processes, in which these proteins participate, might also lead to insights into disease conditions, which involve regulation of actin by Micals and Msrs. |
|---|---|
| AbstractList | Protein structure and function can be regulated via post-translational modifications by numerous enzymatic and nonenzymatic mechanisms. Regulation involving oxidation of sulfur-containing residues emerged as a key mechanism of redox control. Unraveling the participants and principles of such regulation is necessary for understanding the biological significance of redox control of cellular processes.
Reversible oxidation of methionine residues by monooxygenases of the Mical family and subsequent reduction of methionine sulfoxides by a selenocysteine-containing methionine sulfoxide reductase B1 (MsrB1) was found to control the assembly and disassembly of actin in mammals, and the Mical/MsrB pair similarly regulates actin in fruit flies. This finding has opened up new avenues for understanding the use of stereospecific methionine oxidation in regulating cellular processes and the roles of MsrB1 and Micals in regulation of actin dynamics.
So far, Micals have been the only known partners of MsrB1, and actin is the only target. It is important to identify additional substrates of Micals and characterize other Mical-like enzymes.
Oxidation of methionine, reviewed here, is an emerging but not well-established mechanism. Studies suggest that methionine oxidation is a form of oxidative damage of proteins, a modification that alters protein structure or function, a tool in redox signaling, and a mechanism that controls protein function. Understanding the functional impact of reversible oxidation of methionine will require identification of targets, substrates, and regulators of Micals and Msrs. Linking the biological processes, in which these proteins participate, might also lead to insights into disease conditions, which involve regulation of actin by Micals and Msrs. Protein structure and function can be regulated via post-translational modifications by numerous enzymatic and nonenzymatic mechanisms. Regulation involving oxidation of sulfur-containing residues emerged as a key mechanism of redox control. Unraveling the participants and principles of such regulation is necessary for understanding the biological significance of redox control of cellular processes.SIGNIFICANCEProtein structure and function can be regulated via post-translational modifications by numerous enzymatic and nonenzymatic mechanisms. Regulation involving oxidation of sulfur-containing residues emerged as a key mechanism of redox control. Unraveling the participants and principles of such regulation is necessary for understanding the biological significance of redox control of cellular processes.Reversible oxidation of methionine residues by monooxygenases of the Mical family and subsequent reduction of methionine sulfoxides by a selenocysteine-containing methionine sulfoxide reductase B1 (MsrB1) was found to control the assembly and disassembly of actin in mammals, and the Mical/MsrB pair similarly regulates actin in fruit flies. This finding has opened up new avenues for understanding the use of stereospecific methionine oxidation in regulating cellular processes and the roles of MsrB1 and Micals in regulation of actin dynamics.RECENT ADVANCESReversible oxidation of methionine residues by monooxygenases of the Mical family and subsequent reduction of methionine sulfoxides by a selenocysteine-containing methionine sulfoxide reductase B1 (MsrB1) was found to control the assembly and disassembly of actin in mammals, and the Mical/MsrB pair similarly regulates actin in fruit flies. This finding has opened up new avenues for understanding the use of stereospecific methionine oxidation in regulating cellular processes and the roles of MsrB1 and Micals in regulation of actin dynamics.So far, Micals have been the only known partners of MsrB1, and actin is the only target. It is important to identify additional substrates of Micals and characterize other Mical-like enzymes.CRITICAL ISSUESSo far, Micals have been the only known partners of MsrB1, and actin is the only target. It is important to identify additional substrates of Micals and characterize other Mical-like enzymes.Oxidation of methionine, reviewed here, is an emerging but not well-established mechanism. Studies suggest that methionine oxidation is a form of oxidative damage of proteins, a modification that alters protein structure or function, a tool in redox signaling, and a mechanism that controls protein function. Understanding the functional impact of reversible oxidation of methionine will require identification of targets, substrates, and regulators of Micals and Msrs. Linking the biological processes, in which these proteins participate, might also lead to insights into disease conditions, which involve regulation of actin by Micals and Msrs.FUTURE DIRECTIONSOxidation of methionine, reviewed here, is an emerging but not well-established mechanism. Studies suggest that methionine oxidation is a form of oxidative damage of proteins, a modification that alters protein structure or function, a tool in redox signaling, and a mechanism that controls protein function. Understanding the functional impact of reversible oxidation of methionine will require identification of targets, substrates, and regulators of Micals and Msrs. Linking the biological processes, in which these proteins participate, might also lead to insights into disease conditions, which involve regulation of actin by Micals and Msrs. |
| Author | Lee, Byung Cheon Kaya, Alaattin Gladyshev, Vadim N |
| Author_xml | – sequence: 1 givenname: Alaattin surname: Kaya fullname: Kaya, Alaattin organization: 1 Division of Genetics, Department of Medicine, Brigham and Women's Hospital , Harvard Medical School, Boston, Massachusetts – sequence: 2 givenname: Byung Cheon surname: Lee fullname: Lee, Byung Cheon organization: 2 College of Life Sciences and Biotechnology, Korea University , Seoul, South Korea – sequence: 3 givenname: Vadim N surname: Gladyshev fullname: Gladyshev, Vadim N organization: 1 Division of Genetics, Department of Medicine, Brigham and Women's Hospital , Harvard Medical School, Boston, Massachusetts |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/26181576$$D View this record in MEDLINE/PubMed |
| BookMark | eNpNkEtLAzEURoNU7EOXbiVLN1PzmGTSpZb6gIoguh6SyY0dmUlqMiP23zvYFlzdy8e558I3RSMfPCB0ScmcErW40THNGaFiLrkSJ2hChSiyoqBy9G8fo2lKn4QQRik5Q2MmqaKikBMEr_DRN7qrg8fB4W0MHdQeu95Xf5nZ4QjfEFNtGsAtdJshrT3g8FPb_Zn2FncbwDEMxOBI0IAPR9Nzinf0HJ063SS4OMwZer9fvS0fs_XLw9Pydp1Veb7ostwJRqrCaqAgc5CSMmVsYQ04S43iUtCisoYRCyC1NUI55wRn3FpOciXYDF3vvcP3rx5SV7Z1qqBptIfQp5IOXSw4V5wP6NUB7U0LttzGutVxVx6rYb-i5mmY |
| CitedBy_id | crossref_primary_10_1002_ange_202305196 crossref_primary_10_1016_j_psj_2022_101908 crossref_primary_10_1016_j_saa_2024_125464 crossref_primary_10_1038_nchembio_2575 crossref_primary_10_1007_s12011_020_02557_2 crossref_primary_10_1146_annurev_biochem_061516_045037 crossref_primary_10_1016_j_freeradbiomed_2021_05_034 crossref_primary_10_1038_s41598_017_15090_5 crossref_primary_10_1126_science_aal3316 crossref_primary_10_1016_j_bbrc_2017_05_182 crossref_primary_10_1038_s41580_020_0230_3 crossref_primary_10_1107_S2052252519015409 crossref_primary_10_3390_antiox12020401 crossref_primary_10_3233_JAD_180977 crossref_primary_10_1002_ange_202212158 crossref_primary_10_1016_j_abb_2016_08_003 crossref_primary_10_3390_nu13093238 crossref_primary_10_1021_acs_chemrev_7b00698 crossref_primary_10_1038_s41598_017_05230_2 crossref_primary_10_1002_anie_202305196 crossref_primary_10_1016_j_ymeth_2016_06_022 crossref_primary_10_3389_fcell_2021_714370 crossref_primary_10_1002_chem_202002645 crossref_primary_10_3390_antiox11102054 crossref_primary_10_3390_biom11081144 crossref_primary_10_1002_bies_202100096 crossref_primary_10_3390_antiox9101021 crossref_primary_10_1016_j_freeradbiomed_2017_02_010 crossref_primary_10_3390_antiox13121563 crossref_primary_10_3390_horticulturae11040422 crossref_primary_10_1002_biof_1784 crossref_primary_10_1002_iub_1466 crossref_primary_10_1021_jacs_5c02226 crossref_primary_10_3390_antiox11050995 crossref_primary_10_3390_antiox11081613 crossref_primary_10_1016_j_nlm_2019_107104 crossref_primary_10_3390_antiox10050819 crossref_primary_10_1128_AEM_00371_20 crossref_primary_10_1186_s40168_017_0292_4 crossref_primary_10_1016_j_freeradbiomed_2023_05_028 crossref_primary_10_1016_j_bbrc_2017_01_025 crossref_primary_10_1038_s42003_024_07219_w crossref_primary_10_1042_BCJ20170929 crossref_primary_10_1016_j_fct_2020_111938 crossref_primary_10_1007_s12011_019_01881_6 crossref_primary_10_3390_antiox9050383 crossref_primary_10_3390_antiox12040831 crossref_primary_10_1089_ars_2015_6469 crossref_primary_10_1016_j_molp_2017_07_009 crossref_primary_10_1016_j_mito_2020_01_002 crossref_primary_10_1016_j_freeradbiomed_2018_05_076 crossref_primary_10_3390_antiox14060720 crossref_primary_10_3390_antiox10060893 crossref_primary_10_3390_ijms241210109 crossref_primary_10_1016_j_bbagen_2017_02_004 crossref_primary_10_1002_anie_202212158 crossref_primary_10_1016_j_rvsc_2018_10_009 crossref_primary_10_3389_fcell_2023_1263344 crossref_primary_10_1371_journal_pone_0279689 crossref_primary_10_1093_jn_nxac016 crossref_primary_10_1016_j_ejcb_2024_151407 crossref_primary_10_1186_s40104_023_00877_6 crossref_primary_10_1007_s00018_016_2339_2 crossref_primary_10_3390_nu17111902 crossref_primary_10_1038_s41580_024_00730_2 |
| ContentType | Journal Article |
| DBID | CGR CUY CVF ECM EIF NPM 7X8 |
| DOI | 10.1089/ars.2015.6385 |
| DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic |
| DatabaseTitleList | MEDLINE MEDLINE - Academic |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database |
| DeliveryMethod | no_fulltext_linktorsrc |
| Discipline | Medicine Chemistry |
| EISSN | 1557-7716 |
| ExternalDocumentID | 26181576 |
| Genre | Review Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
| GrantInformation_xml | – fundername: NIA NIH HHS grantid: R01 AG021518 – fundername: NIA NIH HHS grantid: AG021518 |
| GroupedDBID | --- 0R~ 23M 4.4 5GY 5RE ABBKN ABJNI ACGFS ACPRK ADBBV AENEX AFOSN AFRAH ALMA_UNASSIGNED_HOLDINGS BNQNF CGR CS3 CUY CVF EBS ECM EIF EJD F5P IER IHR IM4 MV1 NPM NQHIM O9- P2P RML UE5 7X8 IAO SCNPE |
| ID | FETCH-LOGICAL-c449t-4f520c7dae1e64e66128bd7dbefd1b836517cdb20dee6adb58fff5323dd304852 |
| IEDL.DBID | 7X8 |
| ISICitedReferencesCount | 77 |
| ISICitedReferencesURI | http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000361750400005&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| ISSN | 1557-7716 |
| IngestDate | Fri Sep 05 14:27:18 EDT 2025 Thu Jan 02 22:59:55 EST 2025 |
| IsDoiOpenAccess | false |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 10 |
| Language | English |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c449t-4f520c7dae1e64e66128bd7dbefd1b836517cdb20dee6adb58fff5323dd304852 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 |
| PMID | 26181576 |
| PQID | 1716933833 |
| PQPubID | 23479 |
| ParticipantIDs | proquest_miscellaneous_1716933833 pubmed_primary_26181576 |
| PublicationCentury | 2000 |
| PublicationDate | 2015-Oct-01 20151001 |
| PublicationDateYYYYMMDD | 2015-10-01 |
| PublicationDate_xml | – month: 10 year: 2015 text: 2015-Oct-01 day: 01 |
| PublicationDecade | 2010 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States |
| PublicationTitle | Antioxidants & redox signaling |
| PublicationTitleAlternate | Antioxid Redox Signal |
| PublicationYear | 2015 |
| SSID | ssj0002110 |
| Score | 2.4469066 |
| SecondaryResourceType | review_article |
| Snippet | Protein structure and function can be regulated via post-translational modifications by numerous enzymatic and nonenzymatic mechanisms. Regulation involving... |
| SourceID | proquest pubmed |
| SourceType | Aggregation Database Index Database |
| StartPage | 814 |
| SubjectTerms | Adaptor Proteins, Signal Transducing - metabolism Animals Cytoskeletal Proteins - metabolism Humans LIM Domain Proteins - metabolism Methionine - chemistry Methionine - metabolism Methionine Sulfoxide Reductases - metabolism Oxidation-Reduction Oxygenases - metabolism Peroxidase - metabolism Protein Processing, Post-Translational Selenoproteins - chemistry Selenoproteins - metabolism |
| Title | Regulation of protein function by reversible methionine oxidation and the role of selenoprotein MsrB1 |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/26181576 https://www.proquest.com/docview/1716933833 |
| Volume | 23 |
| WOSCitedRecordID | wos000361750400005&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| hasFullText | |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1LS8NAEF7UinrxUV_1xQpeo8km-8hJtFg82FJEobeQfUFBktpU0X_v7CahJ0HwkkMgS5iZnZlvd_g-hK6gLCghtA1UntsgoTkJpGEAVgRLRMyk4tZ7-omPRmIyScfNgVvVjFW2OdEnal0qd0Z-42ldHJ6Kb2fvgVONcrerjYTGKurE0Mq4qOaTJVu4AzeeL5Vy6CIj1nBshiK9AdTo5rroNcQf_b279FVmsPPf_9tF201_ie_qgNhDK6boos1-K-vWRRvD5jZ9H5nnWogeXINLiz1lw7TArtT5d_IbO4KnOeyaN4Od1rQ_vDW4_JrWUkw4LzSGFhK7IUW3htNuKsp2pWE1v48O0Ovg4aX_GDSyC4FKknQRJJaSUHGdm8iwxEABJ0JqrqWxOpLgQBpxpSUJtTEs15IKay2NSax1DPmAkkO0VpSFOUYY0JcFRCIjSQHmsTDlqeVUaSsYJakgPXTZGjMDM7i7irww5UeVLc3ZQ0e1R7JZzb-RAegTEeCkkz98fYq2nJvr8bsz1LGwqc05Wlefi2k1v_DxAs_RePgDGkfL7g |
| linkProvider | ProQuest |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Regulation+of+protein+function+by+reversible+methionine+oxidation+and+the+role+of+selenoprotein+MsrB1&rft.jtitle=Antioxidants+%26+redox+signaling&rft.au=Kaya%2C+Alaattin&rft.au=Lee%2C+Byung+Cheon&rft.au=Gladyshev%2C+Vadim+N&rft.date=2015-10-01&rft.eissn=1557-7716&rft.volume=23&rft.issue=10&rft.spage=814&rft_id=info:doi/10.1089%2Fars.2015.6385&rft_id=info%3Apmid%2F26181576&rft_id=info%3Apmid%2F26181576&rft.externalDocID=26181576 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1557-7716&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1557-7716&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1557-7716&client=summon |