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Control of protein function by prolyl isomerization.

Philipp A M Schmidpeter¹, Johanna R Koch¹, Franz X Schmid¹

¹Laboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth, 95440 Bayreuth, Germany.

Biochimica Et Biophysica Acta

|December 28, 2014

Summary

Prolyl isomerizations are crucial for protein folding and act as molecular timers regulating protein activity. These proline switches offer molecular memory in allosteric systems.

Keywords:

Allostery Prolyl isomerase Protein folding Protein regulation Signaling

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Area of Science:

Biochemistry
Molecular Biology
Cell Signaling

Background:

Prolyl cis/trans isomerizations are essential, rate-limiting steps in protein folding.
These isomerizations are increasingly recognized for their regulatory roles in protein function.

Purpose of the Study:

To elucidate the function of prolyl isomerizations as conformational switches.
To describe specific proline switches and their regulatory mechanisms.

Main Methods:

The study focuses on describing known proline switches and their regulation.
Specific methodologies are not detailed in the abstract but involve analysis of proline-directed processes.

Main Results:

Prolyl isomerizations function as slow conformational switches and molecular timers.
Several examples of regulated proline switches are presented.

Conclusions:

Prolyl isomerizations act as attenuators in biological systems.
They provide molecular memory to allosteric systems, impacting cell signaling.
This research is part of a special issue on Proline-directed Foldases.