gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Synuclein, alpha interacting protein

synphilin-1, synphilin
This gene encodes a protein containing several protein-protein interaction domains, including ankyrin-like repeats, a coiled-coil domain, and an ATP/GTP-binding motif. The encoded protein interacts with alpha-synuclein in neuronal tissue and may play a role in the formation of cytoplasmic inclusions and neurodegeneration. A mutation in this gene has been associated with Parkinson's disease. Alternatively spliced transcript variants encoding different isoforms of this gene have been described, but the full-length nature of only two have been determined. [provided by RefSeq, Jul 2011] (from NCBI)
Top mentioned proteins: alpha-Synuclein, E3 ubiquitin ligase, Ubiquitin, CAN, V1a
Papers using synphilin-1 antibodies
Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
Vandenberghe Wim et al., In The European Journal of Neuroscience, 1999
... was from Exalpha Biologicals; mouse anti-α-tubulin was from Sigma; rabbit anti-α-tubulin and anti-β-tubulin and goat anti-synphilin-1 were from Abcam; rabbit anti-CHIP was from ...
Papers on synphilin-1
Synphilin-1 attenuates mutant LRRK2-induced neurodegeneration in Parkinson's disease models.
Smith et al., Baltimore, United States. In Hum Mol Genet, Feb 2016
Here, using co-immunoprecipitation, we found that LRRK2 interacted with synphilin-1 (SP1), a cytoplasmic protein that interacts with α-synuclein and has implications in PD pathogenesis.
Altered α-synuclein, parkin, and synphilin isoform levels in multiple system atrophy brains.
Pakkenberg et al., Copenhagen, Denmark. In J Neurochem, Jan 2016
Previously, it has been shown that α-synuclein, parkin, and synphilin-1 display disease-specific transcription patterns in frontal cortex in PD, dementia with Lewy bodies, and MSA, and thus may mediate the development of α-synucleinopathies.
RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils.
Sherman et al., Boston, United States. In Embo J, Oct 2015
Mammalian RuvbL associated with the aggresome, and the aggresome substrate synphilin-1 interacted directly with the RuvbL1 barrel-like structure near the opening of the central channel.
Splicing variants of porcine synphilin-1.
Bendixen et al., Århus, Denmark. In Meta Gene, Sep 2015
The presented work reports the molecular cloning and characterization of the porcine (Sus scrofa) synphilin-1 cDNA (SNCAIP) and three splice variants hereof.
Alteration of Upstream Autophagy-Related Proteins (ULK1, ULK2, Beclin1, VPS34 and AMBRA1) in Lewy Body Disease.
Wakabayashi et al., Hirosaki, Japan. In Brain Pathol, Sep 2015
Time course analysis of cultured cells transfected with flag-α-synuclein and synphilin-1 revealed upregulation of these upstream proteins with accumulation of LB-like inclusions.
Expression of Neuronal and Signaling Proteins in Penumbra around a Photothrombotic Infarction Core in Rat Cerebral Cortex.
Uzdensky et al., Rostov-na-Donu, Russia. In Biochemistry (mosc), Jun 2015
The observed upregulation of penumbra proteins involved in maintaining neurite integrity and guidance (NAV3, MAP1, CRMP2, PMP22); intercellular interactions (N-cadherin); synaptic transmission (glutamate decarboxylase, tryptophan hydroxylase, Munc-18-1, Munc-18-3, and synphilin-1); mitochondria quality control and mitophagy (PINK1 and Parkin); ubiquitin-mediated proteolysis and tissue clearance (UCHL1, PINK1, Parkin, synphilin-1); and signaling proteins (PKBα and ERK5) could be associated with tissue recovery.
CCK Response Deficiency in Synphilin-1 Transgenic Mice.
Moran et al., Baltimore, United States. In Plos One, 2014
Previously, we have identified a novel role for the cytoplasmic protein, synphilin-1(SP1), in the controls of food intake and body weight in both mice and Drosophila.
Synphilin-1 binds ATP and regulates intracellular energy status.
Smith et al., Baltimore, United States. In Plos One, 2013
Recent studies have suggested that synphilin-1, a cytoplasmic protein, is involved in energy homeostasis.
The benefits of humanized yeast models to study Parkinson's disease.
Winderickx et al., Leuven, Belgium. In Oxid Med Cell Longev, 2012
More recently, a similar model to study the presumed pathobiology of the α -synuclein interaction partner synphilin-1 has been established.
Use of viral vectors to create animal models for Parkinson's disease.
Aebischer et al., Lausanne, Switzerland. In Neurobiol Dis, 2012
To date, viral PD models comprise α-synuclein and LRRK-2-based overexpression models, as well as models that mimic parkin loss of function by overexpression of the parkin substrates Pael-R, CDCrel-1, p38/JTV or synphilin-1.
Cellular and molecular mechanisms of antioxidants in Parkinson's disease.
Barreto et al., Bogotá, Colombia. In Nutr Neurosci, 2012
Some of the mechanisms reviewed include: scavenging nitrogen and oxygen reactive species, regulation of signaling pathways associated with cell survival and inflammation, and inhibition of synphilin-1 and alpha-synuclein aggregation.
Aggresome formation and segregation of inclusions influence toxicity of α-synuclein and synphilin-1 in yeast.
Franssens et al., Leuven, Belgium. In Biochem Soc Trans, 2011
One of the major hallmarks of PD is the occurrence of intracellular protein deposits in the dying neurons, termed Lewy bodies, which contain different proteins, including aggregated α-synuclein and its interacting protein synphilin-1.
Synphilin-1 inhibits alpha-synuclein degradation by the proteasome.
Castaño et al., Madrid, Spain. In Cell Mol Life Sci, 2011
Synphilin-1 inhibits alpha-synuclein degradation by the proteasome.
Identification of Parkinson's disease candidate genes using CAESAR and screening of MAPT and SNCAIP in South African Parkinson's disease patients.
Bardien et al., Cape Town, South Africa. In J Neural Transm, 2011
Mutation screening of SNCAIP identifies novel sequence variants using a bioinformatic approach; further studies are necessary to determine their possible functional consequences in South African patients with Parkinson's disease.
α-synuclein aggregation reduces nigral myocyte enhancer factor-2D in idiopathic and experimental Parkinson's disease.
Kordower et al., Chicago, United States. In Neurobiol Dis, 2011
Neuronal survival factor MEF2D is decreased in human and experimental Parkinson's disease, a decrease that is specifically associated with alpha-synuclein accumulation and aggregation.
Role of TPPP/p25 on α-synuclein-mediated oligodendroglial degeneration and the protective effect of SIRT2 inhibition in a cellular model of multiple system atrophy.
Takeda et al., Sendai, Japan. In Neurochem Int, 2010
Although serine-129 phosphorylation of alpha-synuclein facilitates tubulin polymerization promoting protein (TPPP)-mediated alpha-SYN oligomerization, this modification does not seem to play an inevitable role in the early step of alpha-SYN oligomer formation.
Deletion of Herp facilitates degradation of cytosolic proteins.
Hori et al., Kanazawa, Japan. In Genes Cells, 2010
Knockdown of Herp gene unexpectedly facilitated the degradation of synphilin-1, and improved cell viability during proteasomal inhibition.
[Alpha-synuclein interacted proteins: the relevance with the pathogenesis of Parkinson's disease].
Jin et al., Hangzhou, China. In Zhejiang Da Xue Xue Bao Yi Xue Ban, 2008
Increasing findings have implicated that some proteins, including parkin, synphilin-1,14-3-3, agrin and tau, interact with alpha-SYN and are involved in the abnormal aggregation of alpha-SYN.
Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease.
Dawson et al., Baltimore, United States. In Nat Med, 2001
Here we show that parkin interacts with and ubiquitinates the alpha-synuclein-interacting protein, synphilin-1.
Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions.
Ross et al., Baltimore, United States. In Nat Genet, 1999
We identified a novel interacting protein, which we term synphilin-1 (encoded by the gene SNCAIP).
share on facebooktweetadd +1mail to friends