2010
DOI: 10.1083/jcb.201001024
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Tubulin polyglutamylation stimulates spastin-mediated microtubule severing

Abstract: Microtubules with long polyglutamylated C-terminal tails are more prone to severing by spastin, establishing the importance of tubulin posttranslational modifications.

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Cited by 271 publications
(293 citation statements)
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“…2). The model is supported by the following data: (1) microtubules treated with subtilisin, a protease that cleaves the unstructured Cterminal tails of tubulin, cannot be severed (McNally and Vale, 1993;Roll-Mecak and Vale, 2005;White et al, 2007); (2) interestingly, the C-terminal tail is where most of the posttranslational modifications of tubulin occur (Verhey and Gaertig, 2007), and certain modifications, such as polyglutamylation, enhance the activity of severing (Lacroix et al, 2010); (3) mutations in the pore-loop region restrict and inhibit severing (Roll-Mecak and Vale, 2008;White et al, 2007) and these same pore mutants are unable to sever microtubules in cells, but are still able to bind and bundle microtubules (White et al, 2007); and (4) antibodies against the C-terminal tails of microtubules block severing activity (Roll-Mecak and Vale, 2008).…”
Section: Introductionmentioning
confidence: 56%
See 1 more Smart Citation
“…2). The model is supported by the following data: (1) microtubules treated with subtilisin, a protease that cleaves the unstructured Cterminal tails of tubulin, cannot be severed (McNally and Vale, 1993;Roll-Mecak and Vale, 2005;White et al, 2007); (2) interestingly, the C-terminal tail is where most of the posttranslational modifications of tubulin occur (Verhey and Gaertig, 2007), and certain modifications, such as polyglutamylation, enhance the activity of severing (Lacroix et al, 2010); (3) mutations in the pore-loop region restrict and inhibit severing (Roll-Mecak and Vale, 2008;White et al, 2007) and these same pore mutants are unable to sever microtubules in cells, but are still able to bind and bundle microtubules (White et al, 2007); and (4) antibodies against the C-terminal tails of microtubules block severing activity (Roll-Mecak and Vale, 2008).…”
Section: Introductionmentioning
confidence: 56%
“…2). Numerous cellular studies have pointed to post-translational modification of the C-terminal tails of tubulin being the greatest indicators of severing activity (Lacroix et al, 2010;Sharma et al, 2007;Sudo and Baas, 2010) (Fig. 2).…”
Section: Introductionmentioning
confidence: 99%
“…It is perhaps surprising that Atat1 knockout mice displayed only minor differences in neurological behaviour. a-tubulin acetylation has been suggested to influence kinesin-mediated transport 10 , and increase sensitivity of microtubules to severing in neuronal axons 43 , although these effects may be more dependent upon other tubulin modifications such as tyrosination 44,45 and polyglutamylation 46 . Migration and maturation of cortical neurons during development have also been reported to be dependent upon tubulin acetylation 14,47 , and depletion of mec17 in zebrafish leads to substantial neurological deficits 17 .…”
Section: Discussionmentioning
confidence: 99%
“…In C. elegans, substitution of a glutamic acid residue in the CTT of ïą-tubulin that is likely to serve in glutamylation rescues the embryonic lethality caused by overproduction of katanin (Lu et al, 2004). Overexpression of the TTLL11 E-ligase in HeLa cells causes fragmentation of microtubules that can be rescued by knockdown of spastin using small interfering RNA (siRNA); moreover, hyperglutamylated microtubules have increased sensitivity to spastin-mediated severing in vitro (Lacroix et al, 2010). Spastin (and probably katanin) are predicted to function as a ring complex of six subunits, with a centrally located pore that incorporates the tubulin CTT (RollMecak and Vale, 2008).…”
Section: Tubulin Ptms Affect the Organization And Dynamics Of Microtumentioning
confidence: 99%