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Neurosci Lett. 2009 Jan 23;450(1):32-6. doi: 10.1016/j.neulet.2008.11.022. Epub 2008 Nov 13.

Myelin basic protein co-distributes with other PI(4,5)P2-sequestering proteins in Triton X-100 detergent-resistant membrane microdomains.

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Department of Molecular and Cellular Biology, University of Guelph, 50 Stone Road East, Guelph, Ontario, Canada.


The 18.5kDa isoform of myelin basic protein (MBP) has recently been shown to sequester phosphatidylinositol-(4,5)-bis-phosphate (PI(4,5)P(2)) in vesicular membranes in vitro, as do domains of other membrane- and cytoskeleton-associated proteins such as MARCKS (myristoylated alanine-rich C kinase substrate) and GAP-43 (growth-associated protein of 43kDa), known collectively as "PI(4,5)P(2)-modulins" [Musse et al., Biochemistry, 47 (2008) 10372-10382 (doi:10.1021/bi801302b)]. Here, we demonstrate co-localisation of MBP and MARCKS in primary rat oligodendrocytes, and co-distribution of MBP, MARCKS, and GAP-43 in lipid raft fractions recovered from Triton X-100 detergent-extracted isolated myelin and brain homogenates. The results lend further support to MBP's multifunctionality, particularly as an additional modulator of PI(4,5)P(2) availability in myelin.

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