FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2003193497> ?p ?o ?g. }

• W2003193497 endingPage "44477" @default.
• W2003193497 startingPage "44471" @default.
• W2003193497 abstract "In neuronal synapses, neurotransmitter-loaded vesicles fuse with presynaptic plasma membrane in a complex sequence of tightly regulated events. The assembly of specialized SNARE complexes plays a pivotal role in this process. The function of the chaperone cysteine string protein α (CSPα) is important for synaptic SNARE complex formation, and mice lacking this protein develop severe synaptic dysfunction and neurodegeneration that lead to their death within 3 months after birth. Another presynaptic protein, α-synuclein, also potentiates SNARE complex formation, and its overexpression rescues the phenotype of CSPα null mutant mice, although these two proteins use different mechanisms to achieve this effect. α-Synuclein is a member of a family of three related proteins whose structural similarity suggests functional redundancy. Here, we assessed whether γ-synuclein shares the ability of α-synuclein to bind synaptic vesicles and ameliorate neurodegeneration caused by CSPα deficiency in vivo. Although the N-terminal lipid-binding domains of the two synucleins showed similar affinity for purified synaptic vesicles, the C-terminal domain of γ-synuclein was not able to interact with synaptobrevin-2/VAMP2. Consequently, overexpression of γ-synuclein did not have any noticeable effect on the phenotype of CSPα null mutant mice. Our data suggest that the functions of α- and γ-synucleins in presynaptic terminals are not fully redundant. In neuronal synapses, neurotransmitter-loaded vesicles fuse with presynaptic plasma membrane in a complex sequence of tightly regulated events. The assembly of specialized SNARE complexes plays a pivotal role in this process. The function of the chaperone cysteine string protein α (CSPα) is important for synaptic SNARE complex formation, and mice lacking this protein develop severe synaptic dysfunction and neurodegeneration that lead to their death within 3 months after birth. Another presynaptic protein, α-synuclein, also potentiates SNARE complex formation, and its overexpression rescues the phenotype of CSPα null mutant mice, although these two proteins use different mechanisms to achieve this effect. α-Synuclein is a member of a family of three related proteins whose structural similarity suggests functional redundancy. Here, we assessed whether γ-synuclein shares the ability of α-synuclein to bind synaptic vesicles and ameliorate neurodegeneration caused by CSPα deficiency in vivo. Although the N-terminal lipid-binding domains of the two synucleins showed similar affinity for purified synaptic vesicles, the C-terminal domain of γ-synuclein was not able to interact with synaptobrevin-2/VAMP2. Consequently, overexpression of γ-synuclein did not have any noticeable effect on the phenotype of CSPα null mutant mice. Our data suggest that the functions of α- and γ-synucleins in presynaptic terminals are not fully redundant." @default.
• W2003193497 created "2016-06-24" @default.
• W2003193497 creator A5005669098 @default.
• W2003193497 creator A5021947706 @default.
• W2003193497 creator A5024445452 @default.
• W2003193497 creator A5026042960 @default.
• W2003193497 creator A5038890837 @default.
• W2003193497 creator A5050460888 @default.
• W2003193497 date "2012-12-01" @default.
• W2003193497 modified "2023-10-18" @default.
• W2003193497 title "Contrasting Effects of α-Synuclein and γ-Synuclein on the Phenotype of Cysteine String Protein α (CSPα) Null Mutant Mice Suggest Distinct Function of these Proteins in Neuronal Synapses" @default.
• W2003193497 cites W1544064013 @default.
• W2003193497 cites W1587973572 @default.
• W2003193497 cites W1844422703 @default.
• W2003193497 cites W1876590017 @default.
• W2003193497 cites W1990473626 @default.
• W2003193497 cites W1991552631 @default.
• W2003193497 cites W1992603978 @default.
• W2003193497 cites W2000119650 @default.
• W2003193497 cites W2005379695 @default.
• W2003193497 cites W2006199861 @default.
• W2003193497 cites W2013593979 @default.
• W2003193497 cites W2017632752 @default.
• W2003193497 cites W2024136850 @default.
• W2003193497 cites W2026169768 @default.
• W2003193497 cites W2032076231 @default.
• W2003193497 cites W2040706104 @default.
• W2003193497 cites W2058394391 @default.
• W2003193497 cites W2058894111 @default.
• W2003193497 cites W2065063347 @default.
• W2003193497 cites W2065393542 @default.
• W2003193497 cites W2068244727 @default.
• W2003193497 cites W2068955183 @default.
• W2003193497 cites W2071087722 @default.
• W2003193497 cites W2074085543 @default.
• W2003193497 cites W2074532659 @default.
• W2003193497 cites W2080566347 @default.
• W2003193497 cites W2091265794 @default.
• W2003193497 cites W2096198116 @default.
• W2003193497 cites W2099976784 @default.
• W2003193497 cites W2113104319 @default.
• W2003193497 cites W2114517395 @default.
• W2003193497 cites W2123184492 @default.
• W2003193497 cites W2128264251 @default.
• W2003193497 cites W2129146981 @default.
• W2003193497 cites W2130323165 @default.
• W2003193497 cites W2138306686 @default.
• W2003193497 cites W2140732014 @default.
• W2003193497 doi "https://doi.org/10.1074/jbc.m112.422402" @default.
• W2003193497 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3531760" @default.
• W2003193497 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23129765" @default.
• W2003193497 hasPublicationYear "2012" @default.
• W2003193497 type Work @default.
• W2003193497 sameAs 2003193497 @default.
• W2003193497 citedByCount "26" @default.
• W2003193497 countsByYear W20031934972013 @default.
• W2003193497 countsByYear W20031934972014 @default.
• W2003193497 countsByYear W20031934972015 @default.
• W2003193497 countsByYear W20031934972016 @default.
• W2003193497 countsByYear W20031934972017 @default.
• W2003193497 countsByYear W20031934972018 @default.
• W2003193497 countsByYear W20031934972019 @default.
• W2003193497 countsByYear W20031934972020 @default.
• W2003193497 countsByYear W20031934972021 @default.
• W2003193497 countsByYear W20031934972022 @default.
• W2003193497 countsByYear W20031934972023 @default.
• W2003193497 crossrefType "journal-article" @default.
• W2003193497 hasAuthorship W2003193497A5005669098 @default.
• W2003193497 hasAuthorship W2003193497A5021947706 @default.
• W2003193497 hasAuthorship W2003193497A5024445452 @default.
• W2003193497 hasAuthorship W2003193497A5026042960 @default.
• W2003193497 hasAuthorship W2003193497A5038890837 @default.
• W2003193497 hasAuthorship W2003193497A5050460888 @default.
• W2003193497 hasBestOaLocation W20031934971 @default.
• W2003193497 hasConcept C130316041 @default.
• W2003193497 hasConcept C134499376 @default.
• W2003193497 hasConcept C142724271 @default.
• W2003193497 hasConcept C148785051 @default.
• W2003193497 hasConcept C170493617 @default.
• W2003193497 hasConcept C200170125 @default.
• W2003193497 hasConcept C2775962898 @default.
• W2003193497 hasConcept C2776219046 @default.
• W2003193497 hasConcept C2776925932 @default.
• W2003193497 hasConcept C2777916540 @default.
• W2003193497 hasConcept C2779134260 @default.
• W2003193497 hasConcept C2779734285 @default.
• W2003193497 hasConcept C2781449126 @default.
• W2003193497 hasConcept C2908790754 @default.
• W2003193497 hasConcept C41625074 @default.
• W2003193497 hasConcept C55493867 @default.
• W2003193497 hasConcept C71924100 @default.
• W2003193497 hasConcept C86803240 @default.
• W2003193497 hasConcept C95444343 @default.
• W2003193497 hasConceptScore W2003193497C130316041 @default.
• W2003193497 hasConceptScore W2003193497C134499376 @default.
• W2003193497 hasConceptScore W2003193497C142724271 @default.
• W2003193497 hasConceptScore W2003193497C148785051 @default.
• W2003193497 hasConceptScore W2003193497C170493617 @default.

• next