Temperature-dependent elasticity of microtubules.
Central to the biological function of microtubules is their ability to modify their length which occurs by addition and removal of subunits at the ends of the polymer, both in vivo and in vitro. This dynamic behavior is strongly influenced by temperature. Here, we show that the lateral interaction between tubulin subunits forming microtubule is strongly temperature dependent. Microtubules deposited on prefabricated substrates were deformed in an atomic force microscope during imaging, in two different experimental geometries. Microtubules were modeled as anisotropic, with the Young's modulus corresponding to the resistance of protofilaments to stretching and the shear modulus describing the weak interaction between the protofilaments. Measurements involving radial compression of microtubules deposited on flat mica confirm that microtubule elasticity depends on the temperature. Bending measurements performed on microtubules deposited on lithographically fabricated substrates show that this temperature dependence is due to changing shear modulus, implying that the lateral interaction between the protofilaments is strongly determined by the temperature. These measurements are in good agreement with previously reported measurements of the disassembly rate of microtubules, demonstrating that the mechanical and dynamic properties of microtubules are closely related.
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Institut de la Physique de la Matière Complexe, EPFL, CH-1015 Lausanne, Switzerland.
Kasas
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Kulik
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Catsicas
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D000818:Animals; D001671:Biochemistry / Q000379:methods; D002417:Cattle; D020285:Cryoelectron Microscopy; D019281:Dimerization; D004548:Elasticity; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D008869:Microtubule-Associated Proteins / Q000737:chemistry; D008870:Microtubules / Q000737:chemistry*; D008968:Molecular Conformation; D013499:Surface Properties; D013696:Temperature; D014404:Tubulin / Q000737:chemistry
D008869:Microtubule-Associated Proteins; D014404:Tubulin