Prion Disease: Exponential Growth Requires Membrane Binding

Prion disease: exponential growth requires membrane binding.

A hallmark feature of prions, whether in mammals or yeast and fungi, is exponential growth associated with fission or autocatalysis of protein aggregates. We have employed a rigorous kinetic analysis to recent data from transgenic mice lacking a glycosylphosphatidylinositol membrane anchor to the normal cellular PrP(C) protein, which show that toxicity requires the membrane binding. We find as ...

Aberrant metal binding by prion protein in human prion disease.

Human prion diseases are characterized by the conversion of the normal prion protein (PrP(C)) into a pathogenic isomer (PrP(Sc)). Distinct PrP(Sc) conformers are associated with different subtypes of prion diseases. PrP(C) binds copper and has antioxidation activity. Changes in metal-ion occupancy can lead to significant decline of the antioxidation activity and changes in conformation of the p...

Normal dynactin complex function during synapse growth in Drosophila requires membrane binding by Arfaptin

Mutations in DCTN1, a component of the dynactin complex, are linked to neurodegenerative diseases characterized by a broad collection of neuropathologies. Because of the pleiotropic nature of dynactin complex function within the neuron, defining the causes of neuropathology in DCTN1 mutants has been difficult. We combined a genetic screen with cellular assays of dynactin complex function to ide...

Membrane Research in a Global Context Requires Collaboration, not Competition!

Familial Prion Disease Cases Without Mutation in PRNPGene

Phosphorus (P), in the form of phosphate ion (Pi), is a vital element contributing in biomolecule structures, metabolic reactions, signaling pathways and energy transfer within the living cells. The objective of the present study was to assess the influence of fungal infection on Pi metabolism in compare to the effects of phosphate stress in Arabidopsis. Quantification of total P contents showe...