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Details on Person Synphilin-1 (SNCAIP) is a presynaptic protein that associate...

Class:IdSummation:5658495
_displayNameSynphilin-1 (SNCAIP) is a presynaptic protein that associate...
_timestamp2015-03-26 10:33:19
created[InstanceEdit:5658493] Jupe, Steve, 2014-12-19
literatureReference[LiteratureReference:5658504] Synphilin-1 is developmentally localized to synaptic terminals, and its association with synaptic vesicles is modulated by alpha-synuclein
[LiteratureReference:5658524] Synphilin-1 is present in Lewy bodies in Parkinson's disease
[LiteratureReference:5658512] Identification and functional characterization of a novel R621C mutation in the synphilin-1 gene in Parkinson's disease
[LiteratureReference:5658502] Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease
[LiteratureReference:5658567] Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation
[LiteratureReference:5658534] Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases
modified[InstanceEdit:5667113] Jupe, Steve, 2015-01-23
[InstanceEdit:5685190] Jupe, Steve, 2015-03-26
textSynphilin-1 (SNCAIP) is a presynaptic protein that associates with synaptic vesicles (Ribeiro et al. 2002). It is present in many types of cytoplasmic inclusions, where it colocalizes with alpha-synuclein (SNCA). It is associated with Parkinson's Disease (PD) because it is an intrinsic component of Lewy bodies (Wakabayashi et al. 2000) and a mutation of the SNCAIP gene has been identified in some PD patients (Marx et al. 2003), suggesting that accumulation of SNCAIP and its interaction with SNCA may be relevant for Lewy body formation in PD.

SNCAIP is ubiquitinated by several different E3 ubiquitin-ligases, including Parkin (PARK2). PARK2 overexpression with SNCAIP in cell culture leads to the formation of protein aggregates (Chung et al. 2001). PARK2 preferentially mediates the addition of lysine-63 (K63)-linked polyubiquitination of SNCAIP (Lim et al. 2005). This leads to SNCAIP degradation only at an unusually high PARK2 to SNCAIP ratio (Lim et al. 2005). K63-linked ubiquitination may be a signal that leads to the degradation of inclusions by autophagy when the ubiquitin-proteasome system is dysfunctional (Lin et al. 2005, Tan et al. 2008).
(summation)[Reaction:5658574] PARK2 binds SNCAIP [Homo sapiens]
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