Control of protein function by prolyl isomerization

• Published in: Biochimica et biophysica acta Vol. 1850; no. 10; pp. 1973 - 1982
• Main Authors: Schmidpeter, Philipp A.M., Koch, Johanna R., Schmid, Franz X.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.10.2015
• Subjects: Allosteric Regulation - physiology; Allostery; Animals; catalysts; drugs; Humans; isomerization; proline; Proline - chemistry; Proline - metabolism; Prolyl isomerase; Protein Folding; Protein regulation; Protein Structure, Tertiary; Proteins - chemistry; Proteins - metabolism; Signaling; Protein regulation; Signaling; Allostery; Protein folding; Prolyl isomerase
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/j.bbagen.2014.12.019

Background: Prolyl cis/trans isomerizations have long been known as critical and rate-limiting steps in protein folding. Results: Now it is clear that they are also used as slow conformational switches and molecular timers in the regulation of protein activity. Here we describe several such proline switches and how they are regulated. Conclusions and general significance: Prolyl isomerizations can function as attenuators and provide allosteric systems with a molecular memory. This article is part of a Special Issue entitled Proline-directed Foldases: Cell Signaling Catalysts and Drug Targets. •Prolyl cis/trans isomerizations are critical and rate-limiting steps in protein folding.•They are also used as slow conformational switches, molecular timers and attenuators.•They provide allosteric proteins with a molecular memory.