Protein-protein interactions involving enzymes of the mammalian methionine and homocysteine metabolism

Enzymes of the methionine and homocysteine metabolism catalyze reactions belonging to the methionine and folate cycles and the transsulfuration pathway. The importance of the metabolites produced through these routes (e.g. S-adenosylmethionine, homocysteine) and their role in e.g. epigenetics or red...

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Detalhes bibliográficos
Autores: Portillo, Francisco, Vázquez, Jesús, Pajares, María Ángeles
Formato: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2020
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/202997
Acesso em linha:http://hdl.handle.net/10261/202997
Access Level:acceso abierto
Palavra-chave:Methionine cycle
S-adenosylmethionine synthesis
Metabolic interplay
Oncogene interactions
Posttranslational modifications
Redox regulation
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spelling Protein-protein interactions involving enzymes of the mammalian methionine and homocysteine metabolismPortillo, FranciscoVázquez, JesúsPajares, María ÁngelesMethionine cycleS-adenosylmethionine synthesisMetabolic interplayOncogene interactionsPosttranslational modificationsRedox regulationEnzymes of the methionine and homocysteine metabolism catalyze reactions belonging to the methionine and folate cycles and the transsulfuration pathway. The importance of the metabolites produced through these routes (e.g. S-adenosylmethionine, homocysteine) and their role in e.g. epigenetics or redox mechanisms makes their tight regulation essential for a correct cellular function. Pharmacological or pathophysiological insults induce, among others, changes in activity, oligomerization, protein levels, subcellular localization and expression of these enzymes. The abundance of these proteins in liver has made this organ the preferred system to study their regulation. Nevertheless, knowledge about their putative protein-protein interactions is limited in this and other tissues and cell types. High-throughput methods, including immunoprecipitation, affinity purification coupled to mass spectrometry and yeast two-hybrid have rendered the identification of a number of protein-protein interactions involving these enzymes in several systems. Validation by coimmunoprecipitation and/or pull-down has been made, mainly, after coexpression of bait and prey, but few of the interactions have been confirmed. Additionally, information concerning the role of these interactions in the regulation of this pathway and other cellular processes is scarce. Here, we review the current knowledge on mammalian protein-protein interactions involving methionine adenosyltransferases, S-adenosylhomocysteine hydrolase, betaine homocysteine S-methyltransferases, methionine synthase and cystathionine β-synthase, although references to data obtained in other organisms are also made. Moreover, the verified or putative implication of these interactions in the regulation of methionine and homocysteine metabolism, its interplay with other metabolic pathways and its putative link to pathophysiological processes, such as oncogenesis, is discussed.This work was supported by grants of the Ministerio de Ciencia,Innovación y Universidades (BFU2005-00050, BFU2008-00666,BFU2009-08977 to MAP; BFU2008-04285 to FP; BIO2015-67580-Pand PGC2018-097019-B-I00 to JV), the Instituto de Salud Carlos III-Fondo de Investigación Sanitaria PRB3 (IPT17/0019-ISCIII-SGEFI/ERDF, ProteoRed to JV), Fundació Marató TV3 (122/C/2015 to JV)and La Caixa Banking Foundation (HR17-00247 to JV). The CNIC issupported by the Instituto de Salud Carlos III (ISCIII), the Ministerio de Ciencia, Innovación y Universidades (MCNU) and the Pro CNIC Foundation, and is a Severo Ochoa Center of Excellence (SEV-2015-0505).Peer reviewedElsevierMinisterio de Ciencia, Innovación y Universidades (España)Instituto de Salud Carlos IIIFundació La Marató de TV3La CaixaFundación Pro CNICPortillo, FranciscoVázquez, Jesús [0000-0003-1461-5092]Pajares, María A. [0000-0002-4714-9051]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202020202020info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/202997reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2015-67580-PMICIU/ICTI2017-2020/PGC2018-097019-B-I00info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/SEV-2015-0505PGC2018-097019-B-I00/AEI/10.13039/501100011033https://doi.org/10.1016/j.biochi.2020.02.015Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2029972026-05-22T06:33:51Z
dc.title.none.fl_str_mv Protein-protein interactions involving enzymes of the mammalian methionine and homocysteine metabolism
title Protein-protein interactions involving enzymes of the mammalian methionine and homocysteine metabolism
spellingShingle Protein-protein interactions involving enzymes of the mammalian methionine and homocysteine metabolism
Portillo, Francisco
Methionine cycle
S-adenosylmethionine synthesis
Metabolic interplay
Oncogene interactions
Posttranslational modifications
Redox regulation
title_short Protein-protein interactions involving enzymes of the mammalian methionine and homocysteine metabolism
title_full Protein-protein interactions involving enzymes of the mammalian methionine and homocysteine metabolism
title_fullStr Protein-protein interactions involving enzymes of the mammalian methionine and homocysteine metabolism
title_full_unstemmed Protein-protein interactions involving enzymes of the mammalian methionine and homocysteine metabolism
title_sort Protein-protein interactions involving enzymes of the mammalian methionine and homocysteine metabolism
dc.creator.none.fl_str_mv Portillo, Francisco
Vázquez, Jesús
Pajares, María Ángeles
author Portillo, Francisco
author_facet Portillo, Francisco
Vázquez, Jesús
Pajares, María Ángeles
author_role author
author2 Vázquez, Jesús
Pajares, María Ángeles
author2_role author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia, Innovación y Universidades (España)
Instituto de Salud Carlos III
Fundació La Marató de TV3
La Caixa
Fundación Pro CNIC
Portillo, Francisco
Vázquez, Jesús [0000-0003-1461-5092]
Pajares, María A. [0000-0002-4714-9051]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Methionine cycle
S-adenosylmethionine synthesis
Metabolic interplay
Oncogene interactions
Posttranslational modifications
Redox regulation
topic Methionine cycle
S-adenosylmethionine synthesis
Metabolic interplay
Oncogene interactions
Posttranslational modifications
Redox regulation
description Enzymes of the methionine and homocysteine metabolism catalyze reactions belonging to the methionine and folate cycles and the transsulfuration pathway. The importance of the metabolites produced through these routes (e.g. S-adenosylmethionine, homocysteine) and their role in e.g. epigenetics or redox mechanisms makes their tight regulation essential for a correct cellular function. Pharmacological or pathophysiological insults induce, among others, changes in activity, oligomerization, protein levels, subcellular localization and expression of these enzymes. The abundance of these proteins in liver has made this organ the preferred system to study their regulation. Nevertheless, knowledge about their putative protein-protein interactions is limited in this and other tissues and cell types. High-throughput methods, including immunoprecipitation, affinity purification coupled to mass spectrometry and yeast two-hybrid have rendered the identification of a number of protein-protein interactions involving these enzymes in several systems. Validation by coimmunoprecipitation and/or pull-down has been made, mainly, after coexpression of bait and prey, but few of the interactions have been confirmed. Additionally, information concerning the role of these interactions in the regulation of this pathway and other cellular processes is scarce. Here, we review the current knowledge on mammalian protein-protein interactions involving methionine adenosyltransferases, S-adenosylhomocysteine hydrolase, betaine homocysteine S-methyltransferases, methionine synthase and cystathionine β-synthase, although references to data obtained in other organisms are also made. Moreover, the verified or putative implication of these interactions in the regulation of methionine and homocysteine metabolism, its interplay with other metabolic pathways and its putative link to pathophysiological processes, such as oncogenesis, is discussed.
publishDate 2020
dc.date.none.fl_str_mv 2020
2020
2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/202997
url http://hdl.handle.net/10261/202997
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2015-67580-P
MICIU/ICTI2017-2020/PGC2018-097019-B-I00
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/SEV-2015-0505
PGC2018-097019-B-I00/AEI/10.13039/501100011033
https://doi.org/10.1016/j.biochi.2020.02.015
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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