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The cellular response to unfolded proteins: intercompartmental signaling

D R McMillan¹, M J Gething, J Sambrook

¹Howard Hughes Medical Institute, Dallas.

Current Opinion in Biotechnology

|October 1, 1994

Summary

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Cells use signaling pathways to manage unfolded proteins in different compartments. Yeast studies reveal a transmembrane receptor regulating endoplasmic reticulum chaperone gene transcription, while E. coli suggests similar prokaryotic pathways.

Area of Science:

Cellular biology
Molecular biology
Biochemistry

Background:

Cells possess mechanisms to respond to unfolded protein accumulation.
Different cellular compartments activate specific stress-responsive genes.
Eukaryotic and prokaryotic cells monitor protein folding status.

Purpose of the Study:

To investigate the mechanisms of unfolded protein response (UPR) signaling.
To identify key regulators of protein folding in cellular compartments.
To explore intercompartmental signaling pathways for unfolded proteins.

Main Methods:

Yeast genetics and molecular biology techniques.
Studies on Escherichia coli signaling pathways.
Analysis of gene transcription in response to protein misfolding.

Related Experiment Videos

Main Results:

A transmembrane receptor in yeast endoplasmic reticulum (ER) monitors chaperone concentration.
This receptor signals to the cytosol to activate nuclear gene transcription for ER chaperones.
Evidence suggests prokaryotes (E. coli) have similar pathways from periplasm/outer membrane to cytoplasm.

Conclusions:

Eukaryotic and prokaryotic cells employ intercompartmental signaling to maintain protein homeostasis.
Transmembrane receptors play a crucial role in sensing and responding to unfolded proteins in specific compartments.
These findings highlight conserved mechanisms for managing cellular stress.