Myelin basic protein: a multifunctional protein

@article{Boggs2006MyelinBP,
  title={Myelin basic protein: a multifunctional protein},
  author={Joan M. Boggs},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={2006},
  volume={63},
  pages={1945-1961}
}
  • J. Boggs
  • Published 23 June 2006
  • Biology, Chemistry
  • Cellular and Molecular Life Sciences CMLS
Abstract.Myelin basic protein (MBP), the second most abundant protein in central nervous system myelin, is responsible for adhesion of the cytosolic surfaces of multilayered compact myelin. A member of the ‘intrinsically disordered’ or conformationally adaptable protein family, it also appears to have several other functions. It can interact with a number of polyanionic proteins including actin, tubulin, Ca2+-calmodulin, and clathrin, and negatively charged lipids, and acquires structure on… 
Interaction of myelin basic protein with cytoskeletal and signaling proteins in cultured primary oligodendrocytes and N19 oligodendroglial cells
TLDR
A role for classic MBP isoforms in protein-protein interactions during membrane and cytoskeletal extension and remodeling in OLGs is supports further a role for MBP associations with these proteins in vivo.
Interaction of myelin basic protein with actin in the presence of dodecylphosphocholine micelles.
TLDR
Whereas the N-terminal domain of MBP can be more important for the MBP's actin polymerization activity and membrane-association, the C-terminAL domain can regulate its interaction with actin.
The Role of Phosphoinositides in the Interaction of Myelin Basic Protein with the Oligodendroglial Cell Membrane
TLDR
It is demonstrated that the signaling lipid phosphatidylinositol (4,5)-bisphosphate (PIP2) is important for the stable association of MBP with cellular membranes and PIP3 play an important role in MBP association to the plasma membrane and oligodendroglial polarity.
The classic basic protein of myelin--conserved structural motifs and the dynamic molecular barcode involved in membrane adhesion and protein-protein interactions.
TLDR
The myelin basic protein (MBP) family comprises a variety of developmentally-regulated members arising from different transcription start sites, differential splicing, and post-translational modifications, and are post-translationally modified to various degrees by methylation, phosphorylation, and deimination.
Structural polymorphism and multifunctionality of myelin basic protein.
TLDR
Biophysical and cell biological approaches are beginning to elucidate the properties of MBP and are leading to a new understanding of the role of this protein as a linker and/or hub in structural and signaling networks in oligodendrocytes and myelin.
Classic 18.5- and 21.5-kDa Myelin Basic Protein Isoforms Associate with Cytoskeletal and SH3-Domain Proteins in the Immortalized N19-Oligodendroglial Cell Line Stimulated by Phorbol Ester and IGF-1
TLDR
A role for classic MBP isoforms in cytoskeletal and other protein-protein interactions during membrane and cytOSkeletal remodeling in OLGs is supported.
Secondary structure and solvent accessibility of a calmodulin-binding C-terminal segment of membrane-associated myelin basic protein.
TLDR
Results confirm both a predicted induced ordering upon membrane association in a specific segment of 18.5 kDa MBP and that this segment is a CaM-binding site, with both interactions weakened by deimination of residues outside of this segment.
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It is thought that while the major MBPs are intracellular adhesion molecules, some of the quantitatively less abundant isoforms that are expressed very early in development may have regulatory effects on the myelination program.
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TLDR
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  • Biology
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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