Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0169-328X(03)00318-8
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dc.titleSEPT5_v2 is a parkin-binding protein
dc.contributor.authorChoi P.
dc.contributor.authorSnyder H.
dc.contributor.authorPetrucelli L.
dc.contributor.authorTheisler C.
dc.contributor.authorChong M.
dc.contributor.authorZhang Y.
dc.contributor.authorLim K.
dc.contributor.authorChung K.K.K.
dc.contributor.authorKehoe K.
dc.contributor.authorD'Adamio L.
dc.contributor.authorLee J.M.
dc.contributor.authorCochran E.
dc.contributor.authorBowser R.
dc.contributor.authorDawson T.M.
dc.contributor.authorWolozin B.
dc.date.accessioned2018-12-27T02:49:57Z
dc.date.available2018-12-27T02:49:57Z
dc.date.issued2003
dc.identifier.citationChoi P., Snyder H., Petrucelli L., Theisler C., Chong M., Zhang Y., Lim K., Chung K.K.K., Kehoe K., D'Adamio L., Lee J.M., Cochran E., Bowser R., Dawson T.M., Wolozin B. (2003). SEPT5_v2 is a parkin-binding protein. Molecular Brain Research 117 (2) : 179-189. ScholarBank@NUS Repository. https://doi.org/10.1016/S0169-328X(03)00318-8
dc.identifier.issn0169328X
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/150218
dc.description.abstractMutations in parkin are associated with various inherited forms of Parkinson's disease (PD). Parkin is a ubiquitin ligase enzyme that catalyzes the covalent attachment of ubiquitin moieties onto substrate proteins destined for proteasomal degradation. The substrates of parkin-mediated ubiquitination have yet to be completely identified. Using a yeast two-hybrid screen, we isolated the septin, human SEPT5_v2 (also known as cell division control-related protein 2), as a putative parkin-binding protein. SEPT5_v2 is highly homologous to another septin, SEPT5, which was recently identified as a target for parkin-mediated ubiquitination. SEPT5_v2 binds to parkin at the amino terminus and in the ring finger domains. Several lines of evidence have validated the putative link between parkin and SEPT5_v2. Parkin co-precipitates with SEPT5_v2 from human substantia nigra lysates. Parkin ubiquitinates SEPT5_v2 in vitro, and both SEPT5_v1 and SEPT5_v2 accumulate in brains of patients with ARJP, suggesting that parkin is essential for the normal metabolism of these proteins. These findings suggest that an important relationship exists between parkin and septins. © 2003 Elsevier B.V. All rights reserved.
dc.publisherElsevier
dc.sourceScopus
dc.subjectAutosomal recessive juvenile Parkinsonism
dc.subjectDegenerative disease: Parkinson's
dc.subjectDisorders of the nervous system
dc.subjectDopamine
dc.subjectDopaminergic neuron
dc.subjectLewy body
dc.subjectParkinson's disease
dc.subjectSubstantia nigra
dc.subjectUbiquitin proteasomal system
dc.subjectUbiquitination
dc.typeArticle
dc.contributor.departmentDEPT OF PHYSIOLOGY
dc.description.doi10.1016/S0169-328X(03)00318-8
dc.description.sourcetitleMolecular Brain Research
dc.description.volume117
dc.description.issue2
dc.description.page179-189
dc.description.codenMBREE
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