How Tubulin Subunits Are Lost from the Shortening Ends of Microtubules

Tran, Phong T.; Joshi, Pallavi; Salmon, Edward D.

doi:10.1006/jsbi.1997.3844

Cited by 86 publications

(90 citation statements)

References 63 publications

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“…Similar observations have been made for CLIP-170 (19). This curved morphology of tubulin oligomers can also be observed in GDP-tubulin rings (20), which is actually the preferred nucleotide state for depolymerized tubulin (21). Furthermore, curved protofilaments are observed at the depolymerizing ends of microtubules (17,22,23).…”

Section: Tubulin Oligomers Function As Intermediates During Polymerizsupporting

confidence: 80%

Structural basis for the extended CAP-Gly domains of p150 ^glued binding to microtubules and the implication for tubulin dynamics

Wang

Crevenna

Kunze

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Significance This study presents a direct visualization of the microtubule-p150glued(CAP-Gly) complex by cryo-EM and seeks to describe the molecular mechanism of the control of tubulin dynamics by p150 CAP-Gly. It highlights the neutralization of the acidic tubulin surface by the basic extensions of CAP-Gly, resulting in the activation of tubulin polymerization. In the condition where the lateral association is impeded (i.e., at low temperature), the extended CAP-Gly domain induces tubulin dimers to connect longitudinally. The two directional modes of self-association of tubulin suggest a foundation for its dynamic behavior at the tip of microtubules and its regulation.

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Section: Tubulin Oligomers Function As Intermediates During Polymerizsupporting

confidence: 80%

Structural basis for the extended CAP-Gly domains of p150 ^glued binding to microtubules and the implication for tubulin dynamics

Wang

Crevenna

Kunze

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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“…Loss of the extensions, often by breakage, correlated with the abrupt onset of polymerization, suggesting that the extensions were nonproductive for polymerization, yet nonpermissive for depolymerization. These extensions differed in radius of curvature by ϳ2 orders of magnitude from the 25-nm-diameter curls of individual GDP tubulin protofilaments induced during the depolymerization phase of microtubule dynamic instability (Mandelkow et al, 1991;Desai et al, 1999b;Tran et al, 1997;Arnal et al, 2000), and although we occasionally saw forked extensions, there was usually one, and never more than two per microtubule end. Colocalization with tubulin fluorescence suggested that these extensions contained tubulin protofilaments (the fluorescence was too weak to conclude unequivocally that these structures were present in the absence of EB1).…”

Section: Does Eb1 Stabilize Protofilament Extensions?mentioning

confidence: 64%

EB1–Microtubule Interactions inXenopusEgg Extracts: Role of EB1 in Microtubule Stabilization and Mechanisms of Targeting to Microtubules

Tirnauer

Grego

Salmon

et al. 2002

MBoC

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125

137

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EB1 targets to polymerizing microtubule ends, where it is favorably positioned to regulate microtubule polymerization and confer molecular recognition of the microtubule end. In this study, we focus on two aspects of the EB1-microtubule interaction: regulation of microtubule dynamics by EB1 and the mechanism of EB1 association with microtubules. Immunodepletion of EB1 from cytostatic factor-arrested M-phase Xenopus egg extracts dramatically reduced microtubule length; this was complemented by readdition of EB1. By time-lapse microscopy, EB1 increased the frequency of microtubule rescues and decreased catastrophes, resulting in increased polymerization and decreased depolymerization and pausing. Imaging of EB1 fluorescence revealed a novel structure: filamentous extensions on microtubule plus ends that appeared during microtubule pauses; loss of these extensions correlated with the abrupt onset of polymerization. Fluorescent EB1 localized to comets at the polymerizing plus ends of microtubules in cytostatic factor extracts and uniformly along the lengths of microtubules in interphase extracts. The temporal decay of EB1 fluorescence from polymerizing microtubule plus ends predicted a dissociation half-life of seconds. Fluorescence recovery after photobleaching also revealed dissociation and rebinding of EB1 to the microtubule wall with a similar half-life. EB1 targeting to microtubules is thus described by a combination of higher affinity binding to polymerizing ends and lower affinity binding along the wall, with continuous dissociation. The latter is likely to be attenuated in interphase. The highly conserved effect of EB1 on microtubule dynamics suggests it belongs to a core set of regulatory factors conserved in higher organisms, and the complex pattern of EB1 targeting to microtubules could be exploited by the cell for coordinating microtubule behaviors.

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“…2B,D). MT ends with curling protofilaments ('ramshorns') in vitro are generally thought to be depolymerising (Simon and Salmon, 1990;Mandelkow et al, 1991;Chretien et al, 1995;Tran et al, 1997a;Müller-Reichert et al, 1998;Arnal et al, 2000;Zovko et al, 2008). Flared protofilaments were 17.7±7.5 nm long (n58), and extended from the MT in a kinked or curved fashion.…”

Section: Growing Microtubule Ends Are Mostly Flaredmentioning

confidence: 99%

Electron tomography reveals a flared morphology on growing microtubule ends

Höög

Huisman

Sebö-Lemke

et al. 2011

Journal of Cell Science

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SummaryMicrotubules (MTs) exhibit dynamic instability, alternating between phases of growth and shortening, mostly at their uncapped plus ends. Based on results from cryo-electron microscopy it was proposed that growing MTs display mainly curved sheets and blunt ends; during depolymerisation curled 'ramshorns' predominate. Observations of MTs in mitotic cells have suggested that the situation in vivo differs from that in vitro, but so far, a clear comparison between in vivo and in vitro results has not been possible because MT end structures could not be correlated directly with the dynamic state of that particular MT. Here we combine light microscopy and electron tomography (ET) to show that growing MT plus ends in the fission yeast Schizosaccharomyces pombe display predominantly a flared morphology. This indicates that MT polymerisation in vivo and in vitro can follow different paths.

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How Tubulin Subunits Are Lost from the Shortening Ends of Microtubules

Cited by 86 publications

References 63 publications

Structural basis for the extended CAP-Gly domains of p150 ^glued binding to microtubules and the implication for tubulin dynamics

Structural basis for the extended CAP-Gly domains of p150 ^glued binding to microtubules and the implication for tubulin dynamics

EB1–Microtubule Interactions inXenopusEgg Extracts: Role of EB1 in Microtubule Stabilization and Mechanisms of Targeting to Microtubules

Electron tomography reveals a flared morphology on growing microtubule ends

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How Tubulin Subunits Are Lost from the Shortening Ends of Microtubules

Cited by 86 publications

References 63 publications

Structural basis for the extended CAP-Gly domains of p150 glued binding to microtubules and the implication for tubulin dynamics

Structural basis for the extended CAP-Gly domains of p150 glued binding to microtubules and the implication for tubulin dynamics

EB1–Microtubule Interactions inXenopusEgg Extracts: Role of EB1 in Microtubule Stabilization and Mechanisms of Targeting to Microtubules

Electron tomography reveals a flared morphology on growing microtubule ends

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Structural basis for the extended CAP-Gly domains of p150 ^glued binding to microtubules and the implication for tubulin dynamics

Structural basis for the extended CAP-Gly domains of p150 ^glued binding to microtubules and the implication for tubulin dynamics