MBP is a peripheral membrane protein, and its interaction with lipids is generally believed to be critical for the formation and stability of the multilamellar myelin sheath. It has been identified as a Ca2+-calmodulin regulated agent for actin polymerization, tropomyosin and actomyosin function, tubulin stabilization, and clathrin assembley. MBP is generally considered to be the antigen responsible for autoimmunity in multiple sclerosis (MS) and it has the capability to induce experimental allergic encephalomyelitis (EAE). MBP is also an endogenous inhibitor of the high-affinity cannabinoid binding site in the brain and a substrate for numerous protein kinases (MAPK, serine/threonine kinase, protein kinase C). MBP is also suggested to be involved in intracellular signalling and as cytoskeletal components.
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