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Article: Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the antiaging and metabolic effects of sirtuins

TitleIdentification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the antiaging and metabolic effects of sirtuins
Authors
KeywordsAffinity chromatography
Aging
Interaction profiling
Ionization time of flight mass spectrometry
Liquid chromatography-tan-dem mass spectrometry
Matrix-assisted laser desorption
Issue Date2009
PublisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/proteomics
Citation
Proteomics, 2009, v. 9 n. 9, p. 2444-2456 How to Cite?
AbstractSirtuins are a family of NAD+-dependent protein deacetylases that regulate cellular functions through deacetylation of a wide range of protein targets. Overexpression of Sir2,the first gene discovered in this family, is able to extend the life span in various organisms. The anti-aging effects of human homologues of sirtuins, SIRT1-7, have also been suggested by animal and human association studies. However, the precise mechanisms whereby sirtuins exert their anti-aging effects remain elusive. In this study, we aim to identify novel interacting partners of SIRT1 and SIRT3, two human sirtuins ubiquitously expressed in many tissue types. Our results demonstrate that SIRT1 and SIRT3 are localized within different intracellular compartments, mainly nuclei and mitochondria, respectively. Using affinity purification and MALDI-TOF/TOF-MS/MS analysis, their potential interacting partners have been identified from the enriched subcellular fractions and specific interactions confirmed by co-immunoprecipitation and Western blotting experiment. Further analyses suggest that overexpression of SIRT1 or SIRT3 in HEK293 cells could induce hypoacetylation and affect the intracellular localizations and protein stabilities of their interacting partners. Taken together, the present study has identified a number of novel SIRT protein interacting partners, which might be critically involved in the anti-aging and metabolic regulatory activities ofsirtuins. © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Persistent Identifierhttp://hdl.handle.net/10722/163247
ISSN
2015 Impact Factor: 4.079
2015 SCImago Journal Rankings: 1.476
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLaw, IKMen_HK
dc.contributor.authorLiu, Len_HK
dc.contributor.authorXu, Aen_HK
dc.contributor.authorLam, KSLen_HK
dc.contributor.authorVanhoutte, PMen_HK
dc.contributor.authorChe, CMen_HK
dc.contributor.authorLeung, PTYen_HK
dc.contributor.authorWang, Yen_HK
dc.date.accessioned2012-09-05T05:29:06Z-
dc.date.available2012-09-05T05:29:06Z-
dc.date.issued2009en_HK
dc.identifier.citationProteomics, 2009, v. 9 n. 9, p. 2444-2456en_HK
dc.identifier.issn1615-9853en_HK
dc.identifier.urihttp://hdl.handle.net/10722/163247-
dc.description.abstractSirtuins are a family of NAD+-dependent protein deacetylases that regulate cellular functions through deacetylation of a wide range of protein targets. Overexpression of Sir2,the first gene discovered in this family, is able to extend the life span in various organisms. The anti-aging effects of human homologues of sirtuins, SIRT1-7, have also been suggested by animal and human association studies. However, the precise mechanisms whereby sirtuins exert their anti-aging effects remain elusive. In this study, we aim to identify novel interacting partners of SIRT1 and SIRT3, two human sirtuins ubiquitously expressed in many tissue types. Our results demonstrate that SIRT1 and SIRT3 are localized within different intracellular compartments, mainly nuclei and mitochondria, respectively. Using affinity purification and MALDI-TOF/TOF-MS/MS analysis, their potential interacting partners have been identified from the enriched subcellular fractions and specific interactions confirmed by co-immunoprecipitation and Western blotting experiment. Further analyses suggest that overexpression of SIRT1 or SIRT3 in HEK293 cells could induce hypoacetylation and affect the intracellular localizations and protein stabilities of their interacting partners. Taken together, the present study has identified a number of novel SIRT protein interacting partners, which might be critically involved in the anti-aging and metabolic regulatory activities ofsirtuins. © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.en_HK
dc.languageengen_US
dc.publisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/proteomicsen_HK
dc.relation.ispartofProteomicsen_HK
dc.subjectAffinity chromatographyen_HK
dc.subjectAgingen_HK
dc.subjectInteraction profilingen_HK
dc.subjectIonization time of flight mass spectrometryen_HK
dc.subjectLiquid chromatography-tan-dem mass spectrometryen_HK
dc.subjectMatrix-assisted laser desorptionen_HK
dc.subject.meshAging - Metabolismen_US
dc.subject.meshCell Lineen_US
dc.subject.meshEscherichia Coli - Geneticsen_US
dc.subject.meshHumansen_US
dc.subject.meshMitochondrial Proteins - Genetics - Metabolismen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Interaction Mapping - Methodsen_US
dc.subject.meshProteins - Metabolismen_US
dc.subject.meshRecombinant Proteins - Genetics - Metabolismen_US
dc.subject.meshSirtuin 1en_US
dc.subject.meshSirtuin 3en_US
dc.subject.meshSirtuins - Genetics - Metabolismen_US
dc.titleIdentification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the antiaging and metabolic effects of sirtuinsen_HK
dc.typeArticleen_HK
dc.identifier.emailXu, A: amxu@hkucc.hku.hken_HK
dc.identifier.emailLam, KSL: ksllam@hku.hken_HK
dc.identifier.emailVanhoutte, PM: vanhoutt@hku.hken_HK
dc.identifier.emailChe, CM: cmche@hku.hken_HK
dc.identifier.emailWang, Y: yuwanghk@hku.hken_HK
dc.identifier.authorityXu, A=rp00485en_HK
dc.identifier.authorityLam, KSL=rp00343en_HK
dc.identifier.authorityVanhoutte, PM=rp00238en_HK
dc.identifier.authorityChe, CM=rp00670en_HK
dc.identifier.authorityWang, Y=rp00239en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1002/pmic.200800738en_HK
dc.identifier.pmid19343720-
dc.identifier.scopuseid_2-s2.0-66249144685en_HK
dc.identifier.hkuros156265-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-66249144685&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume9en_HK
dc.identifier.issue9en_HK
dc.identifier.spage2444en_HK
dc.identifier.epage2456en_HK
dc.identifier.isiWOS:000266318800012-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridLaw, IKM=34872613000en_HK
dc.identifier.scopusauthoridLiu, L=21737444900en_HK
dc.identifier.scopusauthoridXu, A=7202655409en_HK
dc.identifier.scopusauthoridLam, KSL=8082870600en_HK
dc.identifier.scopusauthoridVanhoutte, PM=7202304247en_HK
dc.identifier.scopusauthoridChe, CM=7102442791en_HK
dc.identifier.scopusauthoridLeung, PTY=35740926800en_HK
dc.identifier.scopusauthoridWang, Y=34973733700en_HK
dc.identifier.citeulike7730188-

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