Microtubules cut loose at the cell cortex

David J. Sharp, Brian O'Rourke, Dong Zhang

Research output: Contribution to journalArticle

Abstract

The ability of the microtubule cytoskeleton to rapidly and locally reorganize itself in response to intraand 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 plusends 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.

Original languageEnglish (US)
Pages (from-to)12-15
Number of pages4
JournalFly
Volume6
Issue number1
DOIs
StatePublished - Jan 2012

Fingerprint

microtubules
cortex
cells
cytoskeleton
microfilaments
morphogenesis
cell division
Drosophila
enzymes

Keywords

  • Cell cortex
  • EB1
  • Katanin
  • KLP10A
  • Microtubule

ASJC Scopus subject areas

  • Insect Science

Cite this

Microtubules cut loose at the cell cortex. / Sharp, David J.; O'Rourke, Brian; Zhang, Dong.

In: Fly, Vol. 6, No. 1, 01.2012, p. 12-15.

Research output: Contribution to journalArticle

Sharp, DJ, O'Rourke, B & Zhang, D 2012, 'Microtubules cut loose at the cell cortex', Fly, vol. 6, no. 1, pp. 12-15. https://doi.org/10.4161/fly.18306
Sharp, David J. ; O'Rourke, Brian ; Zhang, Dong. / Microtubules cut loose at the cell cortex. In: Fly. 2012 ; Vol. 6, No. 1. pp. 12-15.
@article{f53e98d4ca744e78aae15041771b5882,
title = "Microtubules cut loose at the cell cortex",
abstract = "The ability of the microtubule cytoskeleton to rapidly and locally reorganize itself in response to intraand 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 plusends 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.",
keywords = "Cell cortex, EB1, Katanin, KLP10A, Microtubule",
author = "Sharp, {David J.} and Brian O'Rourke and Dong Zhang",
year = "2012",
month = "1",
doi = "10.4161/fly.18306",
language = "English (US)",
volume = "6",
pages = "12--15",
journal = "Fly",
issn = "1933-6934",
publisher = "Landes Bioscience",
number = "1",

}

TY - JOUR

T1 - Microtubules cut loose at the cell cortex

AU - Sharp, David J.

AU - O'Rourke, Brian

AU - Zhang, Dong

PY - 2012/1

Y1 - 2012/1

N2 - The ability of the microtubule cytoskeleton to rapidly and locally reorganize itself in response to intraand 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 plusends 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.

AB - The ability of the microtubule cytoskeleton to rapidly and locally reorganize itself in response to intraand 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 plusends 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.

KW - Cell cortex

KW - EB1

KW - Katanin

KW - KLP10A

KW - Microtubule

UR - http://www.scopus.com/inward/record.url?scp=84861421196&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84861421196&partnerID=8YFLogxK

U2 - 10.4161/fly.18306

DO - 10.4161/fly.18306

M3 - Article

C2 - 22388006

AN - SCOPUS:84861421196

VL - 6

SP - 12

EP - 15

JO - Fly

JF - Fly

SN - 1933-6934

IS - 1

ER -