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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

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Engineering allosteric regulation in protein kinases.

David Pincus¹, Jai P Pandey², Zoë A Feder²

¹Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge, MA 02142, USA. pincus@wi.mit.edu kimberly.reynolds@utsouthwestern.edu.

Science Signaling

|November 8, 2018

Summary

This summary is machine-generated.

Researchers identified key "hotspots" on yeast kinases that can be engineered to control cell signaling. This discovery offers insights into allosteric regulation and potential applications in synthetic biology and human disease.

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Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Phosphoregulation is crucial for dynamic cellular responses by modulating protein activity.
Understanding how new phosphoregulation evolves is key to deciphering cellular control mechanisms.

Purpose of the Study:

To identify and characterize novel regulatory sites on yeast kinases.
To engineer new phosphoregulation for rewiring cell signaling pathways.
To explore the role of identified hotspots in allosteric regulation and disease.

Main Methods:

Systematic mutational scanning of yeast kinase surfaces (Kss1).
Engineering of consensus phosphorylation sites at identified regulatory hotspots.
Functional analysis of engineered kinases in yeast signaling pathways.

Main Results:

Discovery of spatially distributed "hotspots" on Kss1 that modulate kinase activity.
Successful rewiring of yeast cell signaling by engineering phosphorylation sites at these hotspots.
Introduction of new phosphoregulation in Hog1, altering its localization and signaling dynamics.

Conclusions:

Identified hotspots represent a conserved mechanism for allosteric regulation in the eukaryotic kinome.
Engineered phosphoregulation at hotspots has potential applications in synthetic biology.
Understanding these hotspots may hold clinical relevance for human diseases, including cancers.