Myelin basic protein: a multifunctional protein
Open accessAbstract
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, Ca(2+)-calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. Some size isoforms of MBP are transported into the nucleus and thus they may also bind polynucleotides. Extracellular signals received by myelin or cultured oligodendrocytes cause changes in phosphorylation of MBP, suggesting that MBP is also involved in signaling. Further study of this very abundant protein will reveal how it is utilized by the oligodendrocyte and myelin for different purposes.
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MBP is the predominant protein within CNS myelin, representing as much as 30% of the protein in myelin, and is essential to myelin formation.
“we chose to label MBP as a putative biological index for myelination because it is the predominant protein within CNS myelin, representing as much as 30% of the protein in myelin (Baumann and Pham-Dinh, 2001) and is essential to myelin formation (Boggs, 2006).”
From The role of myelination in measures of white matter integrity: Combination of diffusion tensor imaging and two-photon microscopy of CLARITY intact brains (2017) · cites this paper as Boggs, 2006
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- Authors
- Boggs, J. M.
- Affiliations
- University of Toronto (CA)
- Corresponding author
- Boggs, J. M.
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2006-06-23
- Volume
- 63
- Issue
- 17
- Pages
- 1945-1961
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC11136439
- OpenAlex
- W1975914956
- Cited by
- 687
- References
- 2
- Citations by year
- 2026: 44 · 2025: 44 · 2024: 65 · 2023: 45 · 2022: 55 · 2021: 46 · 2020: 38 · 2019: 33 · 2018: 26 · 2017: 24 · 2016: 33 · 2015: 25 · 2014: 25 · 2013: 21 · 2012: 34
- FWCI
- 17.95
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cellular and Molecular Life Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Pathology and Forensic Medicine › Multiple Sclerosis Research Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- myelin basic protein, myelin, oligodendrocytes, intrinsically disordered proteins, protein-protein interaction, actin binding, tubulin, calmodulin, clathrin, membrane lipids, tight junctions, nuclear transport, protein phosphorylation, signal transduction, cytoskeleton
- MeSH terms
- Polyelectrolytes, Amino Acid Sequence, Animals, Cytoskeletal Proteins, Myelin Basic Protein, Humans, Lipids, Membrane Lipids, Models, Biological, Molecular Sequence Data, Oligodendroglia, Phosphorylation, Polymers, Protein Processing, Post-Translational, Protein Isoforms, Mice
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