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Analogous standard motifs in myelin basic protein and in MARCKS

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Abstract

Myelin basic protein (MBP) and myristoylated alanine-rich C-kinase substrate (MARCKS) are similar in terms of having extended conformations regulated by their environment (i.e., solubilised or lipid-associated), N-terminal modifications, a dual nature of interactions with lipids, binding to actin and Ca2+-calmodulin, and being substrates for different kinds of protein kinases. The further sequence similarities of segments of MBP with lipid effector regions of MARCKS, and numerous reports in the literature, support the thesis that some developmental isoform of MBP functions in signal transduction.

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  1. Department of Molecular Biology and Genetics, and Biophysics Interdepartmental Group, Univerity of Guelph, Guelph, Ontario, Canada

    George Harauz, Noboru Ishiyama & Ian Bates

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Harauz, G., Ishiyama, N. & Bates, I. Analogous standard motifs in myelin basic protein and in MARCKS. Mol Cell Biochem 209, 155–163 (2000). https://doi.org/10.1023/A:1007176216360

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