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Biochim Biophys Acta Biomembr. 2018 Mar 4. pii: S0005-2736(18)30072-5. doi: 10.1016/j.bbamem.2018.02.031. [Epub ahead of print]

Mechanism of aggregation and membrane interactions of mammalian prion protein.

Author information

1
National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore 560065, India.
2
National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore 560065, India. Electronic address: jayant@ncbs.res.in.

Abstract

The cellular prion protein (PrPC), which is present ubiquitously in all mammalian neurons, is normally found to be linked to the cell membrane through a glycosylphosphatidylinositol (GPI) anchor. The conformational conversion of PrPC into misfolded and aggregated forms is associated with transmissible neurodegenerative diseases known as prion diseases. The importance of different misfolded conformations in prion diseases, and the mechanism by which prion aggregates induce neurotoxicity remain poorly understood. Multiple studies have been shown that the toxicity of misfolded prion protein is directly correlated with its ability to interact with and perturb membranes. This review describes the current progress toward understanding prion protein misfolding and aggregation, as well as the interaction of prion protein aggregates with lipid membrane.

KEYWORDS:

Amyloid; Calcium homeostasis; Ion channel; Lipid membrane; Oligomer; Prion

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