Flexible players within the sheaths : the intrinsically disordered proteins of myelin in health and disease
|Author:||Raasakka, Arne1; Kursula, Petri2|
1Department of Biomedicine, University of Bergen, Jonas Lies vei 91, NO-5009 Bergen, Norway
2Faculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Aapistie 7A, FI-90220 Oulu, Finland
|Online Access:||PDF Full Text (PDF, 6.4 MB)|
|Persistent link:|| http://urn.fi/urn:nbn:fi-fe2020052038536
Multidisciplinary Digital Publishing Institute,
|Publish Date:|| 2020-05-20
Myelin ensheathes selected axonal segments within the nervous system, resulting primarily in nerve impulse acceleration, as well as mechanical and trophic support for neurons. In the central and peripheral nervous systems, various proteins that contribute to the formation and stability of myelin are present, which also harbor pathophysiological roles in myelin disease. Many myelin proteins have common attributes, including small size, hydrophobic segments, multifunctionality, longevity, and regions of intrinsic disorder. With recent advances in protein biophysical characterization and bioinformatics, it has become evident that intrinsically disordered proteins (IDPs) are abundant in myelin, and their flexible nature enables multifunctionality. Here, we review known myelin IDPs, their conservation, molecular characteristics and functions, and their disease relevance, along with open questions and speculations. We place emphasis on classifying the molecular details of IDPs in myelin, and we correlate these with their various functions, including susceptibility to post-translational modifications, function in protein–protein and protein–membrane interactions, as well as their role as extended entropic chains. We discuss how myelin pathology can relate to IDPs and which molecular factors are potentially involved.
|Type of Publication:||
A2 Review article in a scientific journal
|Field of Science:||
1182 Biochemistry, cell and molecular biology
© 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).