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… 
View on Springer
ncbi.nlm.nih.gov
483 Citations
Highly Influential Citations
50
Background Citations
221
Methods Citations
15
Results Citations
2

483 Citations

Citation Type

Citation Type

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.
Myelin basic protein binds microtubules to a membrane surface and to actin filaments in vitro: effect of phosphorylation and deimination.
The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal.
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.
Structured functional domains of myelin basic protein: cross talk between actin polymerization and Ca(2+)-dependent calmodulin interaction.
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.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 193 REFERENCES
Myelin basic protein-diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis.
The Active Transport of Myelin Basic Protein into the Nucleus Suggests a Regulatory Role in Myelination
Membrane adhesion and other functions for the myelin basic proteins
TLDR
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.
Interaction of lipid-bound myelin basic protein with actin filaments and calmodulin.
TLDR
It is shown that MBP bound to acidic lipids can also bind to both G- and F-actin and cause their sedimentation together with MBP-lipid vesicles and its actin binding can be regulated by calmodulin and by the lipid composition of the membrane.
Nuclear transport of myelin basic protein
  • L. Pedraza
  • Biology
    Journal of neuroscience research
  • 1997
TLDR
The intracellular fate of these proteins seems to be generally directed through alternative expression of exon II, and the extent of MBPexII entry into the nucleus was found to be directly related to the growth state of host cells.
Cytoskeleton in myelin-basic-protein-deficient shiverer oligodendrocytes.
TLDR
The shiverer mutant mouse is used to investigate the possible role in cytoskeletal assembly of an MBP gene product or of other myelin components whose expression may be linked to that of MBP.
Expression of myelin basic protein isoforms in nonglial cells
TLDR
It is inferred that the 17- and 21.5-kD MBP isoforms possess strong, nonspecific membrane-binding properties that have been adapted by the oligodendrocyte to mediate compaction of the sheaths of plasma membrane that form myelin.
Effect of arginine loss in myelin basic protein, as occurs in its deiminated charge isoform, on mediation of actin polymerization and actin binding to a lipid membrane in vitro.
TLDR
This posttranslational modification of MBP, which occurs early in life and is increased in multiple sclerosis, attenuates the ability ofMBP to polymerize and bundle actin, and to bind it to a negatively charged membrane.
Three-dimensional Structure of Myelin Basic Protein
TLDR
These results are the first structures achieved directly for this unusual macromolecule, which plays a key role in the development of multiple sclerosis.
Conformation of bovine myelin basic protein purified with bound lipids
TLDR
Theoretical predictions substantially confirm the tendency of the protein to assume an ordered secondary structure in accordance with circular dichroism results, which clearly show that lipid-free MBP is mainly disordered with only a small amount having α-helix and β-sheet motifs.
...
1
2
3
4
5
...