Boggs J M
Department of Structural Biology and Biochemistry, Research Institute, Hospital for Sick Children, Toronto, Ontario, Canada.
Cell Mol Life Sci. 2006 Sep;63(17):1945-61. 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, 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.
髓鞘碱性蛋白（MBP）是中枢神经系统髓鞘中第二丰富的蛋白质，负责多层紧密髓鞘胞质表面的黏附。作为“内在无序”或构象适应性蛋白质家族的一员，它似乎还具有其他多种功能。它可以与多种多阴离子蛋白相互作用，包括肌动蛋白、微管蛋白、Ca(2+)-钙调蛋白和网格蛋白，以及带负电荷的脂质，并在与它们结合时获得结构。它可能作为一种膜肌动蛋白结合蛋白，这可能使其能够参与将细胞外信号传递到少突胶质细胞的细胞骨架和髓鞘中的紧密连接。MBP的一些大小异构体被转运到细胞核中，因此它们也可能与多核苷酸结合。髓鞘或培养的少突胶质细胞接收到的细胞外信号会导致MBP磷酸化的变化，这表明MBP也参与信号传导。对这种非常丰富的蛋白质的进一步研究将揭示少突胶质细胞和髓鞘如何将其用于不同目的。
