Protein self-assembly: A new frontier in cell signaling

Area of Science:

• Biochemistry
• Molecular Biology
• Cell Biology

Background:

• Prions, traditionally considered rare and pathological, are now recognized across all domains of life.
• Specific protein sequences driving prion formation are common in eukaryotes, particularly in proteins involved in information flow and signal transduction.
• Recent research indicates prion formation is a controlled cellular process, not merely random protein misfolding.

Purpose of the Study:

• To review the mechanisms by which protein self-assembly creates a stable record of past stimuli.
• To explore how cellular signaling processes control prion behavior.
• To discuss the implications of prions in biological functions, regulation, and heritable gene expression.

Main Methods:

• Literature review of recent studies on prion formation and function.
• Analysis of protein sequences and their enrichment in specific proteomes.
• Examination of signaling pathways influencing prion behavior.

Main Results:

• Protein self-assembly can serve as a stable cellular memory, altering adaptive responses.
• Prion formation is a regulated process influenced by cellular signals.
• Prions have diverse roles, from fungal drug resistance to human innate immunity.

Conclusions:

• Prion domains in transcription factors and RNA-binding proteins can mediate heritable gene expression changes in response to transient signals.
• Understanding prion mechanisms is crucial for comprehending normal biological regulation and disease.
• The discovery of prions in diverse biological contexts necessitates re-evaluation of their role in cellular information processing.