α-Synuclein Blocks ER-Golgi Traffic and Rab1 Rescues Neuron Loss in Parkinson's Models

By A. Cooper, Aaron Gitler, A. Cashikar, Cole M. Haynes, K. Hill, Bhupinder Bhullar, Kangning Liu, Kexiang Xu, K. Strathearn, Fang Liu and 9 more. Science, 2006

1,354 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Neurology

View Paper: https://www.semanticscholar.org/paper/441cbc0c361a8a1da4103e4679b9833ebe4a10a5

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

In Molecular Biology

In Neurology

Citations in the corpus

Caenorhabditis elegans: An Emerging Model in Biomedical and Environmental Toxicology (2008, background): “Recently, RNAi, genomic, and proteomic approaches using human a-SYNUCLEIN transgenic worms identified genetic networks linking PD to G-protein signaling, endomembrane trafficking, actin cytoskeleton, and oxidative stress (Cooper et al., 2006; Gitler et al., 2008; Hamamichi et al., 2008; Ichibangase ”
Metals, oxidative stress and neurodegenerative disorders (2010, neutral): “The toxic effects of a-synuclein include impaired endoplasmic reticulum (ER) to Golgi vesicular trafficking and ER stress, Golgi fragmentation, sequestration of anti-apoptotic proteins into aggregates, and the formation of pores on cellular membranes [103].”
The Fly as a Model for Neurodegenerative Diseases: Is It Worth the Jump? (2007, neutral): “Geldanamycin is a drug that interferes with the activity of the molecular chaperone Hsp90, which in turn functions as a negative regulator of the heat shock transcription factor that mediates Hsp70 and Hsp40 expression. These observations suggest that chaperones play a significant role in α-synuclei”
α-Synuclein in Parkinson's disease. (2012, background): “This was taken one step further by Cooper et al. (2006), who identified ER-to-Golgi trafficking as the major cellular perturbation in this yeast model, and Rab1, a protein involved in this transition, as a critical determinant of a-synuclein- mediated toxicity in a variety of cellular and in vivo…”
Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities (2008, background): “This occurs perhaps by exhausting proteasome capacity and causing an accumulation of unfolded proteins scheduled for degradation via retrograde translocation from the ER into the cytosol for ubiquitylatio”
Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. (2011, background): “…burden of natural proteins and thus allowed us to study the gain-of-function toxicity caused by aggregation without interference either from loss-of-function alterations or from an augmentation of the biological activities of natural disease proteins (Cooper et al., 2006; Lam et al., 2006).”
Oxidative Stress in Parkinson's Disease: A Mechanism of Pathogenic and Therapeutic Significance (2008, background): “While the precise function of the alpha-synuclein protein remains to be elucidated, there is evidence supporting its involved in pre-synaptic membrane trafficking and neurotransmission [52-54].”