Cold depolymerization of microtubules to double rings: geometric stabilization of assemblies

Melki, Ronald; Carlier, Marie‐France; Pantaloni, Dominique; Timasheff, Serge N.

doi:10.1021/bi00449a028

Cited by 177 publications

(165 citation statements)

References 47 publications

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“…The GDP-GTP exchange (hydrolysis) releases approximately 0.4eV per molecule and is accompanied by a conformational change [18]. This change has been modeled as resulting in a 27 o angle [19] between the original line connecting the centres of the α-and β-monomers and the new centre-to-centre line. These two conformational states and their associated dipole moments have been proposed as the basis for a binary system for information storage and manipulation [17,20].…”

Section: Dipole Moment and Dielectric Properties Of Tubulin Dimersmentioning

confidence: 99%

Surface plasmon resonance study of the actin-myosin sarcomeric complex and tubulin dimers

Schuessler

Mershin²,

Kolomenskii

et al. 2003

Journal of Modern Optics

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Biosensors based on the principle of surface plasmon resonance (SPR) detection were used to measure biomolecular interactions in sarcomeres and changes of the dielectric constant of tubulin samples with varying concentration. At SPR, photons of laser light efficiently excite surface plasmons propagating along a metal (gold) film. This resonance manifests itself as a sharp minimum in the reflection of the incident laser light and occurs at a characteristic angle.The dependence of the SPR angle on the dielectric permittivity of the sample medium adjacent to the gold film allows the monitoring of molecular interactions at the surface. We present results of measurements of cross-bridge attachment/detachment within intact mouse heart muscle sarcomeres and measurements on bovine tubulin molecules pertinent to cytoskeletal signal transduction models.

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Section: Dipole Moment and Dielectric Properties Of Tubulin Dimersmentioning

confidence: 99%

Surface plasmon resonance study of the actin-myosin sarcomeric complex and tubulin dimers

Schuessler

Mershin²,

Kolomenskii

et al. 2003

Journal of Modern Optics

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“…Depolymerizing microtubule ends show characteristic curled protofilaments, whereas relatively straight sheets form at growing ends (3,4). GDP-tubulin does not assemble into microtubules, but forms double rings (5), which also form upon microtubule depolymerization (6) and correspond to curved microtubule protofilaments (7,8). The tendency of GDP-tubulin to curve is thought to strain the microtubule lattice, causing disassembly when the terminal cap of GTP-bound tubulin is lost.…”

mentioning

confidence: 99%

Stathmin and Interfacial Microtubule Inhibitors Recognize a Naturally Curved Conformation of Tubulin Dimers

Barbier

Dorléans

Devred

et al. 2010

Journal of Biological Chemistry

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Tubulin is able to switch between a straight microtubule-like structure and a curved structure in complex with the stathminlike domain of the RB3 protein (T 2 RB3). GTP hydrolysis following microtubule assembly induces protofilament curvature and disassembly. The conformation of the labile tubulin heterodimers is unknown. One important question is whether free GDP-tubulin dimers are straightened by GTP binding or if GTP-tubulin is also curved and switches into a straight conformation upon assembly. We have obtained insight into the bending flexibility of tubulin by analyzing the interplay of tubulinstathmin association with the binding of several small molecule inhibitors to the colchicine domain at the tubulin intradimer interface, combining structural and biochemical approaches. The crystal structures of T 2 RB3 complexes with the chiral R and S isomers of ethyl-5-amino-2-methyl-1,2-dihydro-3-phenylpyrido[3,4-b]pyrazin-7-yl-carbamate, show that their binding site overlaps with colchicine ring A and that both complexes have the same curvature as unliganded T 2 RB3. The binding of these ligands is incompatible with a straight tubulin structure in microtubules. Analytical ultracentrifugation and binding measurements show that tubulin-stathmin associations (T 2 RB3, T 2 Stath) and binding of ligands (R, S, TN-16, or the colchicine analogue MTC) are thermodynamically independent from one another, irrespective of tubulin being bound to GTP or GDP. The fact that the interfacial ligands bind equally well to tubulin dimers or stathmin complexes supports a bent conformation of the free tubulin dimers. It is tempting to speculate that stathmin evolved to recognize curved structures in unassembled and disassembling tubulin, thus regulating microtubule assembly.Microtubules are essential for eukaryotic chromosome segregation, cellular architecture and intracellular trafficking, among other processes. Understanding microtubule dynamics, regulation, and organization requires knowledge of the nucleotide-regulated assembly switch of tubulin. Microtubules are hollow cylinders made of protofilaments of ␣␤-tubulin dimers in head to tail association, forming a pseudohelical lattice (1). The functional assembly-disassembly cycle of a ␣␤-tubulin molecule includes activation by GTP binding at the ␤-subunit, polymerization into microtubules, GTP hydrolysis at the ␤-␣ interdimer interface and depolymerization of GDP-tubulin, followed by replacement by GTP. Vectorial polymerization and GTP hydrolysis combine with tubulin structural plasticity in microtubule dynamics (2). Depolymerizing microtubule ends show characteristic curled protofilaments, whereas relatively straight sheets form at growing ends (3, 4). GDP-tubulin does not assemble into microtubules, but forms double rings (5), which also form upon microtubule depolymerization (6) and correspond to curved microtubule protofilaments (7,8). The tendency of GDP-tubulin to curve is thought to strain the microtubule lattice, causing disassembly when the terminal cap of GTP-bound tubulin...

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“…The switch between the two conformations was postulated to be the driving force for assembly and disassembly (Melki et al 1989, Erickson 1997. The force generated during the disassembly of microtubules could explain the mechanism for chromosome motion (Grishchuk et al 2005, McIntosh et al 2010.…”

Section: Alternating Conformations Of Tubulin and Ftszmentioning

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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Cold depolymerization of microtubules to double rings: geometric stabilization of assemblies

Cited by 177 publications

References 47 publications

Surface plasmon resonance study of the actin-myosin sarcomeric complex and tubulin dimers

Surface plasmon resonance study of the actin-myosin sarcomeric complex and tubulin dimers

Stathmin and Interfacial Microtubule Inhibitors Recognize a Naturally Curved Conformation of Tubulin Dimers

Lessons from bacterial homolog of tubulin, FtsZ for microtubule dynamics

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