Protein intrinsic disorder-based liquid–liquid phase transitions in biological systems: Complex coacervates and membrane-less organelles

2017 ◽  
Vol 239 ◽  
pp. 97-114 ◽  
Author(s):  
Vladimir N. Uversky
Polymers ◽  
2019 ◽  
Vol 11 (6) ◽  
pp. 990 ◽  
Author(s):  
April L. Darling ◽  
Boris Y. Zaslavsky ◽  
Vladimir N. Uversky

The visible outcome of liquid-liquid phase transitions (LLPTs) in cells is the formation and disintegration of various proteinaceous membrane-less organelles (PMLOs). Although LLPTs and related PMLOs have been observed in living cells for over 200 years, the physiological functions of these transitions (also known as liquid-liquid phase separation, LLPS) are just starting to be understood. While unveiling the functionality of these transitions is important, they have come into light more recently due to the association of abnormal LLPTs with various pathological conditions. In fact, several maladies, such as various cancers, different neurodegenerative diseases, and cardiovascular diseases, are known to be associated with either aberrant LLPTs or some pathological transformations within the resultant PMLOs. Here, we will highlight both the physiological functions of cellular liquid-liquid phase transitions as well as the pathological consequences produced through both dysregulated biogenesis of PMLOs and the loss of their dynamics. We will also discuss the potential downstream toxic effects of proteins that are involved in pathological formations.


2008 ◽  
Vol 3 (1) ◽  
pp. 5-28 ◽  
Author(s):  
Ildiko Jancskar ◽  
Amalia Ivanyi

2018 ◽  
Vol 946 ◽  
pp. 012144 ◽  
Author(s):  
V N Naumkin ◽  
A M Lipaev ◽  
V I Molotkov ◽  
D I Zhukhovitskii ◽  
A D Usachev ◽  
...  

Biomolecules ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 1014
Author(s):  
Macy L. Sprunger ◽  
Meredith E. Jackrel

Aberrant protein folding underpins many neurodegenerative diseases as well as certain myopathies and cancers. Protein misfolding can be driven by the presence of distinctive prion and prion-like regions within certain proteins. These prion and prion-like regions have also been found to drive liquid-liquid phase separation. Liquid-liquid phase separation is thought to be an important physiological process, but one that is prone to malfunction. Thus, aberrant liquid-to-solid phase transitions may drive protein aggregation and fibrillization, which could give rise to pathological inclusions. Here, we review prions and prion-like proteins, their roles in phase separation and disease, as well as potential therapeutic approaches to counter aberrant phase transitions.


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