Click
here to close Hello! We notice that
you are using Internet Explorer, which is not supported by Echinobase
and may cause the site to display incorrectly. We suggest using a
current version of Chrome,
FireFox,
or Safari.
Biophys J
2002 Jun 01;826:2916-27. doi: 10.1016/S0006-3495(02)75632-4.
Show Gene links
Show Anatomy links
The importance of lattice defects in katanin-mediated microtubule severing in vitro.
Davis LJ
,
Odde DJ
,
Block SM
,
Gross SP
.
???displayArticle.abstract???
The microtubule-severing enzyme katanin uses ATP hydrolysis to disrupt noncovalent bonds between tubulin dimers within the microtubule lattice. Although its microtubule severing activity is likely important for fundamental processes including mitosis and axonal outgrowth, its mechanism of action is poorly understood. To better understand this activity, an in vitro assay was developed to enable the real-time observation of katanin-mediated severing of individual, mechanically unconstrained microtubules. To interpret the experimental observations, a number of theoretical models were developed and compared quantitatively to the experimental data via Monte Carlo simulation. Models that assumed that katanin acts on a uniform microtubule lattice were incompatible with the in vitro data, whereas a model that assumed that katanin acts preferentially on spatially infrequent microtubule lattice defects was found to correctly predict the experimentally observed breaking rates, number and spatial frequency of severing events, final levels of severing, and sensitivity to katanin concentration over the range 6-300 nM. As a result of our analysis, we propose that defects in the microtubule lattice, which are known to exist but previously not known to have any biological function, serve as sites for katanin activity.
Ahmad,
An essential role for katanin in severing microtubules in the neuron.
1999, Pubmed
Ahmad,
An essential role for katanin in severing microtubules in the neuron.
1999,
Pubmed
Arnal,
How does taxol stabilize microtubules?
1995,
Pubmed
Bell,
Preparation and purification of dynein.
1982,
Pubmed
,
Echinobase
Chrétien,
Lattice defects in microtubules: protofilament numbers vary within individual microtubules.
1992,
Pubmed
Chrétien,
Microtubules switch occasionally into unfavorable configurations during elongation.
2000,
Pubmed
Chrétien,
Limited flexibility of the inter-protofilament bonds in microtubules assembled from pure tubulin.
1998,
Pubmed
Díaz,
Changes in microtubule protofilament number induced by Taxol binding to an easily accessible site. Internal microtubule dynamics.
1998,
Pubmed
Dye,
End-stabilized microtubules observed in vitro: stability, subunit, interchange, and breakage.
1992,
Pubmed
,
Echinobase
Hartman,
Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit.
1998,
Pubmed
,
Echinobase
Hartman,
Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin.
1999,
Pubmed
Hyman,
Structural changes accompanying GTP hydrolysis in microtubules: information from a slowly hydrolyzable analogue guanylyl-(alpha,beta)-methylene-diphosphonate.
1995,
Pubmed
Jánosi,
Modeling elastic properties of microtubule tips and walls.
1998,
Pubmed
Lohret,
A role for katanin-mediated axonemal severing during Chlamydomonas deflagellation.
1998,
Pubmed
Mandelkow,
Microtubule dynamics and microtubule caps: a time-resolved cryo-electron microscopy study.
1991,
Pubmed
McNally,
Capturing a ring of samurai.
2000,
Pubmed
McNally,
Katanin, the microtubule-severing ATPase, is concentrated at centrosomes.
1996,
Pubmed
,
Echinobase
McNally,
Identification of katanin, an ATPase that severs and disassembles stable microtubules.
1993,
Pubmed
,
Echinobase
Müller-Reichert,
Structural changes at microtubule ends accompanying GTP hydrolysis: information from a slowly hydrolyzable analogue of GTP, guanylyl (alpha,beta)methylenediphosphonate.
1998,
Pubmed
Odde,
Diffusion inside microtubules.
1998,
Pubmed
Odde,
Microtubule bending and breaking in living fibroblast cells.
1999,
Pubmed
Simon,
The structure of microtubule ends during the elongation and shortening phases of dynamic instability examined by negative-stain electron microscopy.
1990,
Pubmed
Thorn,
Engineering the processive run length of the kinesin motor.
2000,
Pubmed
Vale,
Severing of stable microtubules by a mitotically activated protein in Xenopus egg extracts.
1991,
Pubmed
Vale,
AAA proteins. Lords of the ring.
2000,
Pubmed
Waterman-Storer,
Actomyosin-based retrograde flow of microtubules in the lamella of migrating epithelial cells influences microtubule dynamic instability and turnover and is associated with microtubule breakage and treadmilling.
1997,
Pubmed
