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Characterization of a MOB1 homolog in the Apicomplexan parasite toxoplasma gondii

dc.contributor.authorDelgado, Inês L. S.
dc.contributor.authorTavares, Alexandra
dc.contributor.authorFrancisco, Samuel
dc.contributor.authorSantos, Dulce
dc.contributor.authorCoelho, João
dc.contributor.authorBasto, Afonso P.
dc.contributor.authorZúquete, Sara
dc.contributor.authorMüller, Joachim
dc.contributor.authorHemphill, Andrew
dc.contributor.authorMeissner, Markus
dc.contributor.authorSoares, Helena
dc.contributor.authorLeitão, Alexandre
dc.contributor.authorNolasco, S.
dc.date.accessioned2021-12-16T15:33:34Z
dc.date.available2021-12-16T15:33:34Z
dc.date.issued2021-11
dc.descriptionFCT_UIDB/00100/2020. FCT_UIDP/00100/2020.pt_PT
dc.description.abstractMonopolar spindle One Binder1 (MOB1) proteins are conserved components of the tumor-suppressing Hippo pathway, regulating cellular processes such as cytokinesis. Apicomplexan parasites present a life cycle that relies on the parasites’ ability to differentiate between stages and regulate their proliferation; thus, Hippo signaling pathways could play an important role in the regulation of the apicomplexan life cycle. Here, we report the identification of one MOB1 protein in the apicomplexan Toxoplasma gondii. To characterize the function of MOB1, we generated gain-of-function transgenic lines with a ligand-controlled destabilization domain, and loss-of-function clonal lines obtained through CRISPR/Cas9 technology. Contrary to what has been characterized in other eukaryotes, MOB1 is not essential for cytokinesis in T. gondii. However, this picture is complex since we found MOB1 localized between the newly individualized daughter nuclei at the end of mitosis. Moreover, we detected a significant delay in the replication of overexpressing tachyzoites, contrasting with increased replication rates in knockout tachyzoites. Finally, using the proximity-biotinylation method, BioID, we identified novel members of the MOB1 interactome, a probable consequence of the observed lack of conservation of some key amino acid residues. Altogether, the results point to a complex evolutionary history of MOB1 roles in apicomplexans, sharing properties with other eukaryotes but also with divergent features, possibly associated with their complex life cycle.pt_PT
dc.description.sponsorshipEXPL/CVT-EPI/1945/2013pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationDelgado IL, Tavares A, Francisco S, Santos D, Soares H, Nolasco S, et al. Characterization of a MOB1 homolog in the Apicomplexan parasite toxoplasma gondii. Biology. 2021;10(12):1233.pt_PT
dc.identifier.doi10.3390/biology10121233pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.21/14064
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.relationFCT_UIDB/00100/2020pt_PT
dc.relationFCT_UIDP/00100/2020pt_PT
dc.relation.publisherversionhttps://www.mdpi.com/2079-7737/10/12/1233pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/pt_PT
dc.subjectToxoplasma gondiipt_PT
dc.subjectTachyzoitept_PT
dc.subjectMOB1pt_PT
dc.subjectHippo pathwaypt_PT
dc.subjectMitotic exit networkpt_PT
dc.subjectApicomplexanpt_PT
dc.subjectEXPL/CVT-EPI/1945/2013pt_PT
dc.subjectFCT_UIDB/00100/2020pt_PT
dc.subjectFCT_UIDP/00100/2020pt_PT
dc.titleCharacterization of a MOB1 homolog in the Apicomplexan parasite toxoplasma gondiipt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/EXPL%2FCVT-EPI%2F1945%2F2013/PT
oaire.citation.issue12pt_PT
oaire.citation.startPage1233pt_PT
oaire.citation.titleBiologypt_PT
oaire.citation.volume10pt_PT
oaire.fundingStream3599-PPCDT
person.familyNameNolasco
person.givenNameSofia
person.identifier.ciencia-id5017-368D-3F71
person.identifier.orcid0000-0003-2168-0511
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication34a552a4-6414-461d-a5f6-862a175ea812
relation.isAuthorOfPublication.latestForDiscovery34a552a4-6414-461d-a5f6-862a175ea812
relation.isProjectOfPublication99775d97-1a92-4d30-b424-1ccabf7ecfb0
relation.isProjectOfPublication.latestForDiscovery99775d97-1a92-4d30-b424-1ccabf7ecfb0

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