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α-Synuclein Promotes SNARE-Complex Assembly in Vivo and in Vitro
Author(s) -
Jacqueline Burré,
Manu Sharma,
Theodoros Tsetsenis,
Vladimir L. Buchman,
Mark R. Etherton,
Thomas C. Südhof
Publication year - 2010
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.1195227
Subject(s) - snare complex , neurodegeneration , microbiology and biotechnology , biology , chaperone (clinical) , syntaxin , synaptobrevin , synaptic vesicle , snap25 , membrane protein , vesicle , biochemistry , membrane , medicine , disease , pathology
α-Synuclein and Aging Transgenic α-synuclein can reverse the otherwise lethal neurodegeneration of cysteine string protein-α knockout mice via changes in SNARE proteins, which mediate synaptic vesicle release. Using experiments with purified recombinant proteins, triple αβγ-synuclein knockout mice, and studies of mouse aging,Burréet al. (p.1663 , published online 26 August) now demonstrate that α-synuclein directly interacts with the SNARE protein synaptobrevin and functions as a catalyst for SNARE-complex assembly. The role of synucleins is fully dispensable in young animals, but becomes essential late in life, which suggests that α-synuclein maintains normal synaptic function during aging.

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