Structural Analysis Of Intermolecular Interactions In The Kinesin Adaptor Complex Fasciculation And Elongation Protein Zeta 1/ Short Coiled-coil Protein (fez1/scoco)

dc.creatorAlborghetti M.R.
dc.creatorFurlan A.d.S.
dc.creatorda Silva J.C.
dc.creatorSforca M.L.
dc.creatorHonorato R.V.
dc.creatorGranato D.C.
dc.creatordos Santos Migueleti D.L.
dc.creatorNeves J.L.
dc.creatorde Oliveira P.S.L.
dc.creatorPaes-Leme A.F.
dc.creatorZeri A.C.M.
dc.creatorde Torriani I.C.L.
dc.creatorKobarg J.
dc.date2013
dc.date2015-06-25T19:10:16Z
dc.date2015-11-26T14:57:18Z
dc.date2015-06-25T19:10:16Z
dc.date2015-11-26T14:57:18Z
dc.date.accessioned2018-03-28T22:09:09Z
dc.date.available2018-03-28T22:09:09Z
dc.identifier
dc.identifierPlos One. , v. 8, n. 10, p. - , 2013.
dc.identifier19326203
dc.identifier10.1371/journal.pone.0076602
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-84885067407&partnerID=40&md5=c36ee05147e95b29401359fc09e031d0
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/88478
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/88478
dc.identifier2-s2.0-84885067407
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1255628
dc.descriptionCytoskeleton and protein trafficking processes, including vesicle transport to synapses, are key processes in neuronal differentiation and axon outgrowth. The human protein FEZ1 (fasciculation and elongation protein zeta 1/ UNC-76, in C. elegans), SCOCO (short coiled-coil protein/ UNC-69) and kinesins (e.g. kinesin heavy chain/ UNC116) are involved in these processes. Exploiting the feature of FEZ1 protein as a bivalent adapter of transport mediated by kinesins and FEZ1 protein interaction with SCOCO (proteins involved in the same path of axonal growth), we investigated the structural aspects of intermolecular interactions involved in this complex formation by NMR (Nuclear Magnetic Resonance), cross-linking coupled with mass spectrometry (MS), SAXS (Small Angle X-ray Scattering) and molecular modelling. The topology of homodimerization was accessed through NMR (Nuclear Magnetic Resonance) studies of the region involved in this process, corresponding to FEZ1 (92-194). Through studies involving the protein in its monomeric configuration (reduced) and dimeric state, we propose that homodimerization occurs with FEZ1 chains oriented in an anti-parallel topology. We demonstrate that the interaction interface of FEZ1 and SCOCO defined by MS and computational modelling is in accordance with that previously demonstrated for UNC-76 and UNC-69. SAXS and literature data support a heterotetrameric complex model. These data provide details about the interaction interfaces probably involved in the transport machinery assembly and open perspectives to understand and interfere in this assembly and its involvement in neuronal differentiation and axon outgrowth. © 2013 Alborghetti et al.
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dc.languageen
dc.publisher
dc.relationPLoS ONE
dc.rightsaberto
dc.sourceScopus
dc.titleStructural Analysis Of Intermolecular Interactions In The Kinesin Adaptor Complex Fasciculation And Elongation Protein Zeta 1/ Short Coiled-coil Protein (fez1/scoco)
dc.typeArtículos de revistas


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