Abstract
Reorganization of microtubules during cell cycle depends on the modulation of activity of microtubule-associated proteins. MAP65 is one of the main microtubule structural proteins in plants responsible for the formation of bundles of parallel and antiparallel microtubules. A member of MAP65 protein family, MAP65-1, binds to microtubules of preprophase band during early stages of cell division and later to the midzone of anaphase spindle and the phragmoplast, but exhibits no or reduced microtubule binding during metaphase. Artificially induced interaction of MAP65-1 with microtubules during metaphase promotes excessive formation of pole-to-pole microtubule bundles and causes delay of anaphase onset. The exact mechanism of this delay is not known, but it was suggested that microtubule bundles induced by MAP65 impose spatial constraints on the chromosome movement obstructing their alignment in the metaphase plate. Interaction of MAP65-1 with microtubules is controlled by phosphorylation. This chapter describes a strategy for the identification of phosphorylation residues responsible for the cell-cycle control of MAP65-1 activity.
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Smertenko, A. (2014). Determination of Phosphorylation Sites in Microtubule Associated Protein MAP65-1. In: Komis, G., Šamaj, J. (eds) Plant MAP Kinases. Methods in Molecular Biology, vol 1171. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-0922-3_13
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DOI: https://doi.org/10.1007/978-1-4939-0922-3_13
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