title: Microtubules cut loose at the cell cortex.
abstract: The ability of the microtubule cytoskeleton to rapidly and locally reorganize itself in response to intra- and extracellular signals is essential to its wide range of functions. A site of tightly regulated microtubule dynamics--and the major interface between the microtubule cytoskeleton and the extracellular environment--is the cell cortex, where the selective stabilization and destabilization of microtubule plus-ends is required for normal cell division, morphogenesis and migration. In a recent study, we found that the cortex of Drosophila S2 and D17 cells is coated with the microtubule severing enzyme and plus-end depolymerase, Kat-60, which actively suppresses microtubule growth and stability along the cell edge. We have proposed that cortical Kat-60 functions by uncapping plus-ends, thereby activating another microtubule depolymerase, KLP10A, preloaded onto the end. The localized destruction of microtubule plus-ends at a specific cortical could feed into larger regulatory pathways, such as those in control of the actin cytoskeleton, to influence cell polarization and motility.
authors.affiliation: Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY, USA.
authors.forename: David J
authors.initials: DJ
authors.lastname: Sharp
authors.forename: Brian
authors.initials: B
authors.lastname: O'Rourke
authors.forename: Dong
authors.initials: D
authors.lastname: Zhang
mesh_terms: D000818:Animals; D003599:Cytoskeleton / Q000378:metabolism; D004330:Drosophila / Q000166:cytology* / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism*; D058105:Polymerization
chemical_list: D008869:Microtubule-Associated Proteins