Exploring the Biological Connection Between Tau and PrP^C in Neuronal Cells: GSK3β as a Possible Key Player.

Area of Science:

• Neuroscience
• Molecular Biology
• Protein Biochemistry

Background:

• Cellular prion protein (PrP^C) and tau are highly expressed in neurons.
• Both proteins play crucial roles in neurogenesis and neuronal differentiation.
• Misfolded PrP^C (PrP^Sc) causes prionopathies, while misfolded tau causes tauopathies, exhibiting prion-like properties.

Purpose of the Study:

• To review the biology and physiological roles of PrP^C and tau in the CNS.
• To explore the molecular convergence points and potential cooperation between PrP^C and tau in neurodegeneration.
• To understand their shared links in natural neuronal physiology.

Main Methods:

• Literature review of existing studies on PrP^C and tau.
• Analysis of molecular interactions and signaling pathways involving PrP^C and tau.
• Discussion of experimental findings on protein splicing and transcriptional regulation.

Main Results:

• PrP^C promotes neuronal differentiation, while tau is essential for axonal maturation.
• PrP^C influences tau alternative splicing by inhibiting GSK3β.
• Tau can regulate the transcription of the PRNP gene, which encodes PrP^C.

Conclusions:

• PrP^C and tau share common molecular pathways and interact in both physiological and pathological contexts.
• Understanding these interactions is crucial for deciphering neurodegenerative mechanisms.
• Further research into the interplay between PrP^C and tau may reveal novel therapeutic targets for prionopathies and tauopathies.