Polyamine Sharing between Tubulin Dimers Favours Microtubule Nucleation and Elongation via Facilitated Diffusion

Alain Mechulam; Konstantin G. Chernov; Elodie Mucher; Loic Hamon; Patrick A. Curmi; David Pastré

doi:10.1371/journal.pcbi.1000255

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Research Article

Polyamine Sharing between Tubulin Dimers Favours Microtubule Nucleation and Elongation via Facilitated Diffusion

Alain Mechulam,

Affiliations Laboratoire Structure-Activité des Biomolécules Normales et Pathologiques, Université Evry-Val d'Essonne, Evry, France, INSERM, U829, Evry, France
⨯
Konstantin G. Chernov,

Affiliations Laboratoire Structure-Activité des Biomolécules Normales et Pathologiques, Université Evry-Val d'Essonne, Evry, France, INSERM, U829, Evry, France, Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia
⨯
Elodie Mucher,

Affiliations Laboratoire Structure-Activité des Biomolécules Normales et Pathologiques, Université Evry-Val d'Essonne, Evry, France, INSERM, U829, Evry, France
⨯
Loic Hamon,

Affiliations Laboratoire Structure-Activité des Biomolécules Normales et Pathologiques, Université Evry-Val d'Essonne, Evry, France, INSERM, U829, Evry, France
⨯
Patrick A. Curmi ,

* E-mail: pcurmi@univ-evry.fr (PAC); david.pastre@univ-evry.fr (DP)

Affiliations Laboratoire Structure-Activité des Biomolécules Normales et Pathologiques, Université Evry-Val d'Essonne, Evry, France, INSERM, U829, Evry, France
⨯
David Pastré

* E-mail: pcurmi@univ-evry.fr (PAC); david.pastre@univ-evry.fr (DP)

Affiliations Laboratoire Structure-Activité des Biomolécules Normales et Pathologiques, Université Evry-Val d'Essonne, Evry, France, INSERM, U829, Evry, France
⨯

Polyamine Sharing between Tubulin Dimers Favours Microtubule Nucleation and Elongation via Facilitated Diffusion

Alain Mechulam,
Konstantin G. Chernov,
Elodie Mucher,
Loic Hamon,
Patrick A. Curmi,
David Pastré

Published: January 2, 2009
https://doi.org/10.1371/journal.pcbi.1000255

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An image is associated with this article

Posted by PLOS_CompBiol on 19 Jan 2009 at 14:45 GMT

We suggest for the first time that the action of multivalent cations on
microtubule dynamics can result from facilitated diffusion of GTP-tubulin to the
microtubule ends.
http://ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.1000255#article1.front1.article-meta1.abstract1.p1

In this work, "facilitated diffusion" is introduced as a novel view on microtubule assembly. Facilitated diffusion states that polycations (like natural polyamines) generate an attraction force between tubulin molecules and microtubules. The attracted tubulin molecules can eventually diffuse to microtubule ends and thus increase the rate of microtubule elongation. Together the results modify our vision of microtubule assembly and provide a novel target to manipulate microtubule dynamics for pharmacologic purposes.

View the image here:
http://www.ploscompbiol.org/attachments/pcbi.1000255.facilitatedDiffusion.tif

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Tubulins
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Microtubules
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Polyamine Sharing between Tubulin Dimers Favours Microtubule Nucleation and Elongation via Facilitated Diffusion

Polyamine Sharing between Tubulin Dimers Favours Microtubule Nucleation and Elongation via Facilitated Diffusion

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An image is associated with this article

Posted by PLOS_CompBiol on 19 Jan 2009 at 14:45 GMT