Evolving Tip Structures Can Explain Age-Dependent Microtubule Catastrophe

Coombes, Courtney; Yamamoto, Ami; Kenzie, Madeline R.; Odde, David J.; Gardner, Melissa K.

doi:10.1016/j.cub.2013.05.059

Cited by 124 publications

(215 citation statements)

References 33 publications

(60 reference statements)

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“…S2A]. Here, the "dim" end of the microtubule is likely composed of variable protofilament lengths (26)(27)(28), and thus may expose the internal microtubule luminal surface (Fig. 1B, cartoon), an effect that may be enhanced by the microtubule depolymerizing properties of αTAT1 (29) (SI Appendix, Fig.…”

Section: Resultsmentioning

confidence: 99%

Mechanism of microtubule lumen entry for the α-tubulin acetyltransferase enzyme αTAT1

Coombes

Yamamoto

McClellan

et al. 2016

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

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113

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Microtubules are structural polymers inside of cells that are subject to posttranslational modifications. These posttranslational modifications create functionally distinct subsets of microtubule networks in the cell, and acetylation is the only modification that takes place in the hollow lumen of the microtubule. Although it is known that the α-tubulin acetyltransferase (αTAT1) is the primary enzyme responsible for microtubule acetylation, the mechanism for how αTAT1 enters the microtubule lumen to access its acetylation sites is not well understood. By performing biochemical assays, fluorescence and electron microscopy experiments, and computational simulations, we found that αTAT1 enters the microtubule lumen through the microtubule ends, and through bends or breaks in the lattice. Thus, microtubule structure is an important determinant in the acetylation process. In addition, once αTAT1 enters the microtubule lumen, the mobility of αTAT1 within the lumen is controlled by the affinity of αTAT1 for its acetylation sites, due to the rapid rebinding of αTAT1 onto highly concentrated α-tubulin acetylation sites. These results have important implications for how acetylation could gradually accumulate on stable subsets of microtubules inside of the cell.microtubule | acetylation | biophysics | microscopy | modeling

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Section: Resultsmentioning

confidence: 99%

Mechanism of microtubule lumen entry for the α-tubulin acetyltransferase enzyme αTAT1

Coombes

Yamamoto

McClellan

et al. 2016

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

Self Cite

113

View full text Add to dashboard Cite

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“…MT plus ends can also be blunt when protofilaments are of almost equal length and remain parallel to each other. New MTs have been shown, both experimentally and in simulation, to initiate growth with a metastable blunt end that is recalcitrant to catastrophe and to gradually become more dynamic with frequent tapered ends (Gardner et al, 2012;Coombes et al, 2013). In MTs of the Arabidopsis phragmoplast, the blunt ends are often associated with cell plate membranes and thus appear to be static (Austin et al, 2005).…”

Section: Tubulin Heterogeneitymentioning

confidence: 99%

Microtubules in Plants

Hashimoto

2015

The Arabidopsis Book

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Microtubules (MTs) are highly conserved polar polymers that are key elements of the eukaryotic cytoskeleton and are essential for various cell functions. αβ-tubulin, a heterodimer containing one structural GTP and one hydrolysable and exchangeable GTP, is the building block of MTs and is formed by the sequential action of several molecular chaperones. GTP hydrolysis in the MT lattice is mechanistically coupled with MT growth, thus giving MTs a metastable and dynamic nature. MTs adopt several distinct higher-order organizations that function in cell division and cell morphogenesis. Small molecular weight compounds that bind tubulin are used as herbicides and as research tools to investigate MT functions in plant cells. The de novo formation of MTs in cells requires conserved γ-tubulin-containing complexes and targeting/activating regulatory proteins that contribute to the geometry of MT arrays. Various MT regulators and tubulin modifications control the dynamics and organization of MTs throughout the cell cycle and in response to developmental and environmental cues. Signaling pathways that converge on the regulation of versatile MT functions are being characterized.

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“…Catastrophe was said to be linked to the 'aging' of the microtubule tips (Coombes et al 2013). As the microtubule grows, the tips become tapered with time, and this change is independent of the hydrolysis of GTP.…”

Section: Dynamics Of Assemblymentioning

confidence: 99%

“…As the microtubule grows, the tips become tapered with time, and this change is independent of the hydrolysis of GTP. Proteins that modify the microtubule tip structures might promote the catastrophe (Coombes et al 2013).…”

Section: Dynamics Of Assemblymentioning

confidence: 99%

Lessons from bacterial homolog of tubulin, FtsZ for microtubule dynamics

Battaje

Panda

2017

Endocrine-Related Cancer

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FtsZ, a homolog of tubulin, is found in almost all bacteria and archaea where it has a primary role in cytokinesis. Evidence for structural homology between FtsZ and tubulin came from their crystal structures and identification of the GTP box. Tubulin and FtsZ constitute a distinct family of GTPases and show striking similarities in many of their polymerization properties. The differences between them, more so, the complexities of microtubule dynamic behavior in comparison to that of FtsZ, indicate that the evolution to tubulin is attributable to the incorporation of the complex functionalities in higher organisms. FtsZ and microtubules function as polymers in cell division but their roles differ in the division process. The structural and partial functional homology has made the study of their dynamic properties more interesting. In this review, we focus on the application of the information derived from studies on FtsZ dynamics to study microtubule dynamics and vice versa. The structural and functional aspects that led to the establishment of the homology between the two proteins are explained to emphasize the network of FtsZ and microtubule studies and how they are connected.

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Evolving Tip Structures Can Explain Age-Dependent Microtubule Catastrophe

Cited by 124 publications

References 33 publications

Mechanism of microtubule lumen entry for the α-tubulin acetyltransferase enzyme αTAT1

Mechanism of microtubule lumen entry for the α-tubulin acetyltransferase enzyme αTAT1

Microtubules in Plants

Lessons from bacterial homolog of tubulin, FtsZ for microtubule dynamics

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