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Myelin‐specific proteins: A structurally diverse group of membrane‐interacting molecules
Author(s) -
Han Huijong,
Myllykoski Matti,
Ruskamo Salla,
Wang Chaozhan,
Kursula Petri
Publication year - 2013
Publication title -
biofactors
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.204
H-Index - 94
eISSN - 1872-8081
pISSN - 0951-6433
DOI - 10.1002/biof.1076
Subject(s) - myelin , proteolipid protein 1 , myelin associated glycoprotein , glycoprotein , microbiology and biotechnology , oligodendrocyte , citrullination , biology , myelin sheath , myelin oligodendrocyte glycoprotein , membrane protein , biophysics , myelin basic protein , biochemistry , chemistry , neuroscience , membrane , central nervous system , amino acid , arginine , citrulline
Abstract The myelin sheath is a multilayered membrane in the nervous system, which has unique biochemical properties. Myelin carries a set of specific high‐abundance proteins, the structure and function of which are still poorly understood. The proteins of the myelin sheath are involved in a number of neurological diseases, including autoimmune diseases and inherited neuropathies. In this review, we briefly discuss the structural properties and functions of selected myelin‐specific proteins (P0, myelin oligodendrocyte glycoprotein, myelin‐associated glycoprotein, myelin basic protein, myelin‐associated oligodendrocytic basic protein, P2, proteolipid protein, peripheral myelin protein of 22 kDa, 2′,3′‐cyclic nucleotide 3′‐phosphodiesterase, and periaxin); such properties include, for example, interactions with lipid bilayers and the presence of large intrinsically disordered regions in some myelin proteins. A detailed understanding of myelin protein structure and function at the molecular level will be required to fully grasp their physiological roles in the myelin sheath. © 2013 BioFactors, 2013