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Automated Imaging and Analysis for the Quantification of Fluorescently Labeled Macropinosomes

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Peptides induce persistent signaling from endosomes by a nutrient transceptor.

Marta Rubio-Texeira¹, Griet Van Zeebroeck, Johan M Thevelein

¹Laboratory of Molecular Cell Biology, Institute of Botany and Microbiology, KU Leuven, Flanders, Belgium.

Nature Chemical Biology

|March 6, 2012

Summary

Specific dipeptides persistently activate yeast protein kinase A by disrupting Gap1 transceptor sorting. This novel mechanism involves pH-sensitive proton influx, leading to endosomal accumulation and sustained signaling.

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Area of Science:

Cellular Biology
Molecular Biology
Yeast Genetics

Background:

The yeast Gap1 transceptor is crucial for amino acid sensing and activates the protein kinase A (PKA) pathway.
Gap1 undergoes endocytic internalization after amino acid transport, a process typically leading to vacuolar sorting.
Transceptors are membrane proteins that link transport activity to intracellular signaling pathways.

Purpose of the Study:

To identify novel agonists that modulate Gap1 transceptor activity and signaling.
To investigate the mechanism by which Gap1 internalization and signaling are regulated.
To characterize the impact of specific dipeptides on Gap1 trafficking and PKA activation.

Main Methods:

Yeast genetics and mutant analysis (e.g., blocking multivesicular body sorting).
Biochemical assays to measure protein kinase A (PKA) activation.
Analysis of Gap1 localization using endosomal and vacuolar markers.
Transport assays to study dipeptide uptake and pH sensitivity.

Main Results:

Three specific γ-glutamyl dipeptides were identified as persistent agonists of Gap1, causing sustained PKA activation independent of cyclic AMP.
These dipeptides prevented Gap1 vacuolar sorting, leading to its accumulation in endosomes.
Dipeptide uptake was mediated by Gap1, sensitive to external pH, and induced intracellular acidification, suggesting proton influx.
High external pH, NHA1 deletion, or V-ATPase inhibition restored Gap1 vacuolar sorting.

Conclusions:

Specific dipeptides act as persistent agonists for the Gap1 transceptor, decoupling transport from normal trafficking.
Enhanced proton influx through Gap1, triggered by these dipeptides, causes defective vacuolar sorting and sustained signaling.
This study reveals a novel mechanism of transceptor regulation and persistent signaling mediated by specific transported molecules.