@article{09a3dd39185f4a0a8fc3291d41a15640,
title = "The life of a microtubule",
author = "Ram Dixit and Sabine Petry",
note = "Funding Information: Once a MT has grown, its length and the total number of MTs can be tuned to suit cellular needs. The MT-severing protein, katanin, has emerged as a key regulator of these processes, but the structural basis for how this MT scissor operates and the molecular mechanisms that target and regulate severing activity remain unclear. Graham Burkart (Dixit laboratory, Washington University in St. Louis) presented data that showed that the evolutionarily conserved MAP65 family of MT cross-linking proteins potently protect the sidewalls of MTs against severing by inhibiting the binding of katanin. Insight into how katanin performs its severing activity was provided by Elena Zehr (Roll-Mecak laboratory, National Institutes of Health). Her elegant cryo–electron microscopy and x-ray crystallography work showed that katanin alternates between an open-spiral and closed-ring state in an ATP-dependent manner that is proposed to represent the power stroke that mediates MT severing. In contrast to katanin, the CLASP family of proteins act as MT rescue factors. While the domain architectures of yeast CLASP and XMAP215 are similar, Shreoshi Majumdar (Rice laboratory, University of Texas Southwestern Medical Center) reported that the single TOG2 domain of CLASP was sufficient for rescue activity, unlike XMAP215, which requires two TOG domains for its MT polymerase activity. Her work shed light on structural differences that might account for the inherent functional differences between the CLASP TOG2 and polymerase TOGs.",
year = "2018",
month = mar,
day = "15",
doi = "10.1091/mbc.E17-11-0677",
language = "English (US)",
volume = "29",
pages = "689",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "American Society for Cell Biology",
number = "6",
}