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The Journal of Neuroscience, September 1, 2002, 22(17):7398-7407

Myelin Proteolipid Protein Forms a Complex with Integrins and May Participate in Integrin Receptor Signaling in Oligodendrocytes

Tatyana I. Gudz¹, Tracy E. Schneider¹, Thomas A. Haas², and Wendy B. Macklin¹

Departments of ¹ Neurosciences and ² Molecular Cardiology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195

Myelination of axons in the CNS by oligodendrocytes is a process critical to rapid and efficient impulse conduction. A new role for the myelin proteolipid protein (PLP), the most abundant protein of CNS myelin, has been identified, in studies showing PLP interaction with signaling proteins in oligodendrocytes. In particular, these studies suggest that the PLP protein may be involved in signaling through integrins in oligodendrocytes. Stimulation of muscarinic acetylcholine receptors on oligodendrocytes induced formation of a tripartite complex containing PLP, calreticulin, and _v-integrin. PLP interacted directly with the cytoplasmic domain of the _v-integrin. Complex formation was mediated by phospholipase C and Ca²⁺ binding to the high affinity binding site on calreticulin. This complex appears important for binding of fibronectin to oligodendrocytes. These data establish a novel function for PLP as a part of the integrin signaling complex in oligodendrocytes and suggest that neurotransmitter-mediated integrin receptor signaling may be involved in myelinogenesis.

Key words: oligodendrocyte; myelin; proteolipid protein; integrin; calreticulin; muscarinic; acetylcholine receptor

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Copyright © 2002 Society for Neuroscience  0270-6474/02/22177398-10$05.00/0

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