Cellular prion protein （PrP^C） widely exists in mammals as a transmembrane glycoprotein， and gene-knockout studies have shown that PrP^C plays a key role in the activity of the nervous system， including peripheral nerve myelination and protection against neurotoxic stimuli. PrP^C has different biological functions in different cell types. With the features of a modular structure， multiple binding partners， and close association with lipid rafts， PrP^C has the function to assemble multicomponent complexes， trigger different signaling pathways， and regulate cell differentiation. No consensus has been reached on the pathological role of PrP^C in the brain， and the scrapie isoform of the prion protein （PrP^SC） formed by misfolding is a main pathogenic factor for prion diseases. However， evidence has shown that the pathogenic effect of PrP^C in prion diseases is independent of PrP^SC， and during prion infection， clinical and neuropathological symptoms of prion diseases are positively correlated with the expression of PrP^C rather than PrP^SC. In addition， PrP^C may also be a protein associated with neurodegenerative diseases and participates in the neurotoxic signal transduction for protein aggregates including β-amyloid， and it also acts as a cellular receptor of α-synuclein to promote its cell uptake and spread in the brain. Although great achievements have been made in the research on prion， the role of PrP^C in brain remains unclear， and therefore， it is of great significance to explore the role of PrP^C in cells.Journal of International Neurology and Neurosurgery, 2021, 48(1): 86-89］