The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model
By Michelle onPublished: Tau neuronal aggregation is a driver of some neurodegenerative disorders. These toxic aggregates form when affected cells release aggregate seeds which are then internalized by unaffected cells. The authors show that a protein,Clusterin, delays Tau aggregation and suppresses seeding activity. View original preprint.
The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends
By Michelle onPublished: Irreversible toxic aggregates are a hallmark of neurodegenerative diseases, such as alpha-synuclein in PD. Using microfluidic diffusional sizing, the authors show that the molecular chaperone family Hsp70 (specifically Hsc70, DnaJB, and Apg2) can completely dissolve alpha-synuclein aggregation and revert it back to its monomeric state.
Quantitative proteomics reveals the selectivity of ubiquitin-binding autophagy receptors in the turnover of damaged lysosomes by lysophagy
By Michelle onPublished: The authors used proteomics to develop a quantitative snapshot of the proteins involved in lysophagy. Among the proteins identified, they found that TAX1BP1 and TBK1 are both required for lysophagy. View original preprint.
Hippocampal Neuronal Culture
By Blythe Lloyd onThis protocol describes the procedure for hippocampal neuronal cultures from new - born mouse pups.
In situ architecture of neuronal α-Synuclein inclusions
By Michelle onPublished: Alpha-synuclein aggregation has been associated with Parkinson’s disease. Using cutting-edge imaging tools, the authors show neuronal alpha-synuclein inclusions within their native states. Further, they show that these aggregates are intermixed with cellular organelles and how aggregation spreads across the brain. View original preprint.
Vesicular dysfunction and pathways to neurodegeneration
By Michelle onIn this review, the pathways that have emerged as being critical for neuronal survival in the human brain is be discussed – illustrating the diversity of proteins and cellular events with three molecular case studies drawn from different neurological diseases.
A possible role for VPS13-family proteins in bulk lipid transfer, membrane expansion, and organelle biogenesis.
By Blythe Lloyd onReview: This review focuses on the structure and function of the VPS13 family of proteins and discusses the prevailing hypthoses in the field regarding its role in lipid transport.
From structure to ætiology: a new window on the biology of leucine-rich repeat kinase 2 and Parkinson’s disease
By Michelle onReview: This review summarizes LRRK2 structure both in a historical and current context, highlighting new insights into the structure of LRRK2 and complexes it forms.
Integrating protein networks and machine learning for disease stratification in the Hereditary Spastic Paraplegias
By Michelle onPublished: Hereditary Spastic Paraplegias are a group of neurodegenerative disorders with diverse clinical presentation and genetic variability. The authors used validated human data to create a protein-protein interaction map using causative genes to identify core proteins and processes. View original preprint.
Insights into VPS13 properties and function reveal a new mechanism of eukaryotic lipid transport
By Blythe Lloyd onReview: This review focuses on the disssecting the VPS13 family of proteins and their novel role in mediating lipid transfer between organelles.