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Volume 271, Number 44, Issue of November 1, 1996 pp. 27838-27846
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Myelin Proteolipid Protein (PLP), but Not DM-20, Is an Inositol Hexakisphosphate-binding Protein

(Received for publication, February 28, 1996, and in revised form, August 14, 1996)

Yoshihide Yamaguchi , Kazuhiro Ikenaka , Michio Niinobe ^¶ , Hitoshi Yamada and Katsuhiko Mikoshiba ^''

From the  Laboratory of Neural Information, National Institute for Physiological Sciences, Okazaki National Research Institutes, Okazaki, Aichi 444, the ^¶ Division of Regulation of Macromolecular Function, Institute for Protein Research, Osaka University, Suita, Osaka 565, the  Molecular Neurobiology Laboratory, Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), Tsukuba, Ibaragi 305, and the ^'' Department of Molecular Neurobiology, Institute of Medical Science, University of Tokyo, Minato-Ku, Tokyo 108, Japan

Myelin proteolipid protein (PLP) and its alternatively spliced isoform, DM-20, are the major integral membrane proteins of central nervous system myelin. It is known that PLP and DM-20 are delivered to myelin by a finely regulated vesicular transport system in oligodendrocytes. Evolutionarily, it is believed that ancestral DM-20 acquired a PLP-specific exon to create PLP, after which PLP/DM-20 became a major component of central nervous system myelin. We purified PLP as an inositol 1,3,4,5-tetrakisphosphate-binding protein after solubilization in a non-organic solvent. However, under the isotonic condition, PLP binds inositol hexakisphosphate (InsP₆) significantly, not inositol 1,3,4,5-tetrakisphosphate. Most of the InsP₆-binding proteins are involved in vesicular transport, suggesting the involvement of PLP in vesicular transport. We separated DM-20 from PLP by CM-52 chromatography and showed that DM-20 has no InsP₆ binding activity. These findings indicate that the PLP-specific domain confers the InsP₆ binding activity and this interaction may be important for directing PLP transport to central nervous system myelin.

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