Cellular and Molecular Life Sciences CMLS

, Volume 63, Issue 17, pp 1945–1961

Myelin basic protein: a multifunctional protein


DOI: 10.1007/s00018-006-6094-7

Cite this article as:
Boggs, J.M. Cell. Mol. Life Sci. (2006) 63: 1945. doi:10.1007/s00018-006-6094-7


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 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.


Intrinsically unstructuredcytoskeletoncalmodulinlipid vesicledeiminationphosphorylationoligodendrocytemultiple sclerosis

Copyright information

© Birkhäuser Verlag, Basel 2006

Authors and Affiliations

  1. 1.Department of Structural Biology and Biochemistry, Research InstituteHospital for Sick ChildrenTorontoCanada
  2. 2.Department of Laboratory Medicine and PathobiologyUniversity of TorontoTorontoCanada