Abstract
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.
Highlights
IntroductionThe vertebrate nervous system has evolved to serve a vast diversity of animals, including humans
The vertebrate nervous system has evolved to serve a vast diversity of animals, including humans.The brain and the spinal cord form the central nervous system (CNS), which orchestrates information storage and processing, as well as reads sensory output
While non-compact myelin contains both “typical” soluble and membrane proteins, compact myelin contains a mere handful of proteins, some specific to CNS or peripheral nervous system (PNS), which are capped by one attribute over others: molecular weight
Summary
The vertebrate nervous system has evolved to serve a vast diversity of animals, including humans. Non-compactmyelin myelinlines linesthe theouterouter-and andinnermost innermostlayers layersofofmyelin, myelin,known knownas asthe theabaxonal abaxonaland and It forms paranodal loops—structures at the ends of the adaxonal layers, respectively. Inthethe are known as Schmidt–Lanterman and longitudinal incisures, Water is abundant inabundant non-compact myelin, which contains cytoskeletal elements and servesand as a respectively. The and narrow extracellular space signaling adhesion take place [14].between the periodic compact myelin membranes is called the intramyelinic compartment. Theleaflet myelin membrane formed is asymmetric: the extracellular/intramyelinic monolayer is rich in glycolipids, whereas the cytoplasmic leaflet is predominantly formed of phospholipids and harbors a net negative charge [17]. Giant leaps in myelin protein research have been taken in recent years, especially in the study of myelin intrinsically disordered proteins (IDPs), which are the main focus of this review
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