Please use this identifier to cite or link to this item: https://doi.org/10.2755/jcmm010.004.04
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dc.titleα - synuclein and Parkinson's disease: The first roadblock
dc.contributor.authorLin Chua, C.E.
dc.contributor.authorTang, B.L.
dc.date.accessioned2014-11-26T07:49:28Z
dc.date.available2014-11-26T07:49:28Z
dc.date.issued2006-10
dc.identifier.citationLin Chua, C.E., Tang, B.L. (2006-10). α - synuclein and Parkinson's disease: The first roadblock. Journal of Cellular and Molecular Medicine 10 (4) : 828-837. ScholarBank@NUS Repository. https://doi.org/10.2755/jcmm010.004.04
dc.identifier.issn15821838
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/109740
dc.description.abstractα-synuclein gene mutations are major underlying genetic defects known in familial juvenile onset Parkinson's disease (PD), and α-synuclein is a major constituent of Lewy Bodies, the pathological hallmark of PD. The normal cellular function of α-synuclein has been elusive, and its exact etiological mechanism in causing dopaminergic neuronal death in PD is also not clearly understood. Very recent reports now indicate that mutant or simply over-expressed α-synuclein could cause damage by interfering with particular steps of neuronal membrane traffic. α-synuclein selectively blocks endoplamic reticulum-to-Golgi transport, thus causing ER stress. A screen in a yeast revealed that α-synuclein toxicity could be suppressed by over-expression of the small GTPase Ypt1/Rab1, and that over-expression of the latter rescues neuron loss in invertebrate and mammalian models of α-synuclein-induced neurodegeneration. α-synuclein may also serve a chaperone function for the proper folding of synaptic SNAREs that are important for neurotransmitter release. We discuss these recent results and the emerging pathophysiological interaction of α-synuclein with components of neuronal membrane traffic.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.2755/jcmm010.004.04
dc.sourceScopus
dc.subjectα-synuclein
dc.subjectEndoplasmic reticulum
dc.subjectGolgi
dc.subjectMembrane traffic
dc.subjectParkinson's disease
dc.typeArticle
dc.contributor.departmentBIOCHEMISTRY
dc.description.doi10.2755/jcmm010.004.04
dc.description.sourcetitleJournal of Cellular and Molecular Medicine
dc.description.volume10
dc.description.issue4
dc.description.page828-837
dc.identifier.isiut000242876700003
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