The Schizosaccharomyces pombe EB1 homolog Mal3p binds and stabilizes the microtubule lattice seam. Export

@article{citeulike:1428314, abstract = {End binding 1 (EB1) proteins are highly conserved regulators of microtubule dynamics. Using electron microscopy (EM) and high-resolution surface shadowing we have studied the microtubule-binding properties of the fission yeast EB1 homolog Mal3p. This allowed for a direct visualization of Mal3p bound on the surface of microtubules. Mal3p particles usually formed a single line on each microtubule along just one of the multiple grooves that are formed by adjacent protofilaments. We provide structural data showing that the alignment of Mal3p molecules coincides with the microtubule lattice seam as well as data suggesting that Mal3p not only binds but also stabilizes this seam. Accordingly, Mal3p stabilizes microtubules through a specific interaction with what is potentially the weakest part of the microtubule in a way not previously demonstrated. Our findings further suggest that microtubules exhibit two distinct reaction platforms on their surface that can independently interact with target structures such as microtubule-associated proteins, motors, kinetochores, or membranes.}, address = {Structural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.}, author = {Sandblad, L. and Busch, K. E. and Tittmann, P. and Gross, H. and Brunner, D. and Hoenger, A.}, citeulike-article-id = {1428314}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.cell.2006.11.025}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/17190604}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=17190604}, citeulike-linkout-3 = {http://www.sciencedirect.com/science/article/B6WSN-4MP07P3-J/1/b196987a43c22cd9b3850463ce5cf352}, day = {29}, doi = {10.1016/j.cell.2006.11.025}, issn = {0092-8674}, journal = {Cell}, keywords = {dynamics, imaging, lattice, microtubule, pombe}, month = {December}, number = {7}, pages = {1415--1424}, posted-at = {2007-07-02 10:57:15}, priority = {2}, title = {The Schizosaccharomyces pombe EB1 homolog Mal3p binds and stabilizes the microtubule lattice seam.}, url = {http://dx.doi.org/10.1016/j.cell.2006.11.025}, volume = {127}, year = {2006} }

TY - JOUR ID - citeulike:1428314 L3 - citeulike-article-id:1428314 N2 - End binding 1 (EB1) proteins are highly conserved regulators of microtubule dynamics. Using electron microscopy (EM) and high-resolution surface shadowing we have studied the microtubule-binding properties of the fission yeast EB1 homolog Mal3p. This allowed for a direct visualization of Mal3p bound on the surface of microtubules. Mal3p particles usually formed a single line on each microtubule along just one of the multiple grooves that are formed by adjacent protofilaments. We provide structural data showing that the alignment of Mal3p molecules coincides with the microtubule lattice seam as well as data suggesting that Mal3p not only binds but also stabilizes this seam. Accordingly, Mal3p stabilizes microtubules through a specific interaction with what is potentially the weakest part of the microtubule in a way not previously demonstrated. Our findings further suggest that microtubules exhibit two distinct reaction platforms on their surface that can independently interact with target structures such as microtubule-associated proteins, motors, kinetochores, or membranes. IS - 7 JF - Cell SN - 0092-8674 AD - Structural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany. EP - 1424 TI - The Schizosaccharomyces pombe EB1 homolog Mal3p binds and stabilizes the microtubule lattice seam. VL - 127 SP - 1415 KW - dynamics KW - imaging KW - lattice KW - microtubule KW - pombe AU - Sandblad, L AU - Busch, KE AU - Tittmann, P AU - Gross, H AU - Brunner, D AU - Hoenger, A PY - 2006/12/29/ UR - http://dx.doi.org/10.1016/j.cell.2006.11.025 ER -