MxA interacts with and is modified by the SUMOylation machinery

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorBrantis-de-Carvalho, Carlos Eduardo
dc.creatorMaarifi, Ghizlane
dc.creatorGonçalves Boldrin, Paulo Eduardo
dc.creatorZanelli, Cleslei Fernando
dc.creatorNisole, Sebastien
dc.creatorChelbi-Alix, Mounira K.
dc.creatorValentini, Sandro Roberto
dc.date2015-10-21T20:57:08Z
dc.date2016-10-25T21:09:01Z
dc.date2015-10-21T20:57:08Z
dc.date2016-10-25T21:09:01Z
dc.date2015-01-01
dc.date.accessioned2017-04-06T09:09:19Z
dc.date.available2017-04-06T09:09:19Z
dc.identifierExperimental Cell Research. San Diego: Elsevier Inc, v. 330, n. 1, p. 151-163, 2015.
dc.identifier0014-4827
dc.identifierhttp://hdl.handle.net/11449/129372
dc.identifierhttp://acervodigital.unesp.br/handle/11449/129372
dc.identifierhttp://dx.doi.org/10.1016/j.yexcr.2014.10.020
dc.identifierWOS:000348411500013
dc.identifierhttp://www.sciencedirect.com/science/article/pii/S0014482714004819
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/939927
dc.descriptionMx proteins are evolutionarily conserved dynamin-like large GTPases involved in viral resistance triggered by types I and III interferons. The human MxA is a cytoplasmic protein that confers resistance to a large number of viruses. The MxA protein is also known to self-assembly into high molecular weight homo-oligomers. Using a yeast two-hybrid screen, we identified 27 MxA binding partners, some of which are related to the SUMOylation machinery. The interaction of MxA with Small-Ubiquitin MOdifier 1 (SUMO1) and Ubiquitin conjugating enzyme 9 (Ubc9) was confirmed by co-immunoprecipitation and co-localization by confocal microscopy. We identified one SUMO conjugation site at lysine 48 and two putative SUMO interacting motifs (SIMa and SIMb). We showed that MxA interacts with the EIL loop of SUMO1 in a SIM-independent manner via its CID-GED domain. The yeast two-hybrid mapping also revealed that Ubc9 binds to the MxA GTPase domain. Mutation in the putative SIMa and SIMb, which are located in the GTPase binding domain, reduced MxA antiviral activity. In addition, we showed that MxA can be conjugated to SUMO2 or SUMO3 at lysine 48 and that the SUMOylation-deficient mutant of MxA (MxA(K48R)) retained its capacity to oligomerize and to inhibit Vesicular Stomatitis Virus (VSV) and Influenza A Virus replication, suggesting that MxA SUMOylation is not essential for its antiviral activity. (C) 2014 Elsevier Inc. All rights reserved.
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.languageeng
dc.publisherElsevier B.V.
dc.relationExperimental Cell Research
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectMX1
dc.subjectMxA
dc.subjectYeast two-hybrid
dc.subjectSUMOylation
dc.subjectEIL loop
dc.subjectSUMO
dc.subjectUbc9 and antiviral activity
dc.titleMxA interacts with and is modified by the SUMOylation machinery
dc.typeOtro


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