Human FEZ1 Protein Forms a Disulfide Bond Mediated Dimer: Implications for Cargo Transport

dc.creatorAlborghetti, MR
dc.creatorFurlan, AS
dc.creatorSilva, JC
dc.creatorLeme, AFP
dc.creatorTorriani, ICL
dc.creatorKobarg, J
dc.date2010
dc.dateSEP
dc.date2014-11-14T14:54:46Z
dc.date2015-11-26T17:15:25Z
dc.date2014-11-14T14:54:46Z
dc.date2015-11-26T17:15:25Z
dc.date.accessioned2018-03-29T00:03:40Z
dc.date.available2018-03-29T00:03:40Z
dc.identifierJournal Of Proteome Research. Amer Chemical Soc, v. 9, n. 9, n. 4595, n. 4603, 2010.
dc.identifier1535-3893
dc.identifierWOS:000281443700025
dc.identifier10.1021/pr100314q
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/68899
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/68899
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/68899
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1282042
dc.descriptionThe human proteins FEZ1 (fasciculation and elongation protein zeta 1) and FEZ2 are orthologs of the protein UNC-76 from C. elegans, involved in the growth and fasciculation of the worms axon. Pull down assays showed that the protein FEZ1 interacts with other proteins (e.g., the protein SCOCO, short coiled-coil protein), mitochondria, and vesicles. These components may therefore represent cargoes to be transported along the microtubule, and the transport may be mediated through FEZ1 reported binding to kinesins (KIF3A). We previously showed that FEZ1 dimerizes in its N-terminal region and interacts with other proteins, including the candidate cargoe proteins, through its C-terminus. Here, we studied the fragment FEZ1(92-194) as well as full-length 6xHis-FEZ1 (1-392) in vitro and endogenous FEZ1 isolated from HEK 293 cells and were able to demonstrate the formation of an intermolecular disulfide bond through FEZ1 Cys-133, which appears to be essential for dimerization. This disulfide bond may be important for the FEZ1 role as a dimeric and bivalent transport adaptor molecule, since it establishes a strong link between the monomers, which could be a prerequisite for the simultaneous binding of two cargoes.
dc.description9
dc.description9
dc.description4595
dc.description4603
dc.descriptionFundacao de Amparo a Pesquisa do Estado Sao Paulo
dc.descriptionConselho Nacional de Pesquisa e Desenvolvimento
dc.descriptionLNBio-CNPEM
dc.languageen
dc.publisherAmer Chemical Soc
dc.publisherWashington
dc.publisherEUA
dc.relationJournal Of Proteome Research
dc.relationJ. Proteome Res.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectneuron
dc.subjecthomodimer
dc.subjectdisulfide bond
dc.subjectcargo transport
dc.subjectmicrotubules
dc.subjectkinesin
dc.subjectSAXS
dc.subjectFEZ1
dc.subjectflower-like phenotype
dc.subjectNatively Unfolded Protein
dc.subjectInteracting Protein
dc.subjectSolution Scattering
dc.subjectAxonal Outgrowth
dc.subjectResolution
dc.subjectKinesin
dc.subjectUnc-76
dc.subjectDomain
dc.subjectGene
dc.subjectMicrotubules
dc.titleHuman FEZ1 Protein Forms a Disulfide Bond Mediated Dimer: Implications for Cargo Transport
dc.typeArtículos de revistas


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