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

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 oligod...

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Bibliographic Details
Published in:The Journal of neuroscience 2002-09, Vol.22 (17), p.7398-7407
Main Authors: Gudz, Tatyana I, Schneider, Tracy E, Haas, Thomas A, Macklin, Wendy B
Format: Article
Language:English
Subjects:
Animals
Antigens, CD - metabolism
Calcium - metabolism
Calcium-Binding Proteins - metabolism
Calreticulin
Cells, Cultured
Enzyme Inhibitors - pharmacology
Extracellular Matrix Proteins - metabolism
Integrin alphaV
Integrins - metabolism
Macromolecular Substances
Muscarinic Agonists - pharmacology
Myelin Proteolipid Protein - metabolism
Oligodendroglia - cytology
Oligodendroglia - drug effects
Oligodendroglia - metabolism
Precipitin Tests
Protein Binding
Rats
Receptors, Cell Surface - metabolism
Ribonucleoproteins - metabolism
Signal Transduction - drug effects
Signal Transduction - physiology
Type C Phospholipases - antagonists & inhibitors
Type C Phospholipases - metabolism
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Summary: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 alpha(v)-integrin. PLP interacted directly with the cytoplasmic domain of the alpha(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.
ISSN:0270-6474
1529-2401
DOI:10.1523/jneurosci.22-17-07398.2002