QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online November 24, 2004
doi: 10.1242/10.1242/jcs.01531

This Article Figures Only Full Text Full Text (PDF) Supplementary Material Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Samsonov, A. Articles by Popov, S. V. Search for Related Content PubMed PubMed Citation Articles by Samsonov, A. Articles by Popov, S. V.

Tau interaction with microtubules in vivo

¹ Department of Physiology and Biophysics M/C 901, University of Illinois at Chicago, 835 S. Wolcott Avenue, Chicago, IL 60612, USA
² Department of Psychiatry M/C 901, University of Illinois at Chicago, 835 S. Wolcott Avenue, Chicago, IL 60612, USA

^* Author for correspondence (e-mail: spopov{at}uic.edu)

Accepted 13 September 2004

Tau is a major microtubule-associated protein which induces bundling and stabilization of axonal microtubules (MTs). To investigate the interaction of tau with MTs in living cells, we expressed GFP-tau fusion protein in cultured Xenopus embryo neurons and performed time-lapse imaging of tau-labeled MTs. Tau uniformly labeled individual MTs regardless of their assembly/disassembly status and location along the axon. Photobleaching experiments indicated that interaction of tau with MTs is very dynamic, with a half-time of fluorescence recovery of the order of 3 seconds. Treatment of cells with taxol, a drug that suppresses MT dynamics, rapidly induced detachment of tau from MTs. Although binding of tau to straight MTs was uniform, there was a heightened concentration of tau at the sites of high MT curvature. Our results suggest that dynamic interaction of tau with MTs may modify local mechanical properties of individual MTs and play a crucial role in the remodeling of the MT cytoskeleton during neuronal plasticity.

Key words: Microtubule, Tau, Axon, Tubulin, Photobleaching, Rigidity

This article has been cited by other articles:

				J. J. Lee and S. M. Swain The Epothilones: Translating from the Laboratory to the Clinic Clin. Cancer Res., March 15, 2008; 14(6): 1618 - 1624. [Abstract] [Full Text] [PDF]

				S. Konzack, E. Thies, A. Marx, E.-M. Mandelkow, and E. Mandelkow Swimming against the Tide: Mobility of the Microtubule-Associated Protein Tau in Neurons J. Neurosci., September 12, 2007; 27(37): 9916 - 9927. [Abstract] [Full Text] [PDF]

				A. Oladipo, A. Cowan, and V. Rodionov Microtubule Motor Ncd Induces Sliding of Microtubules In Vivo Mol. Biol. Cell, September 1, 2007; 18(9): 3601 - 3606. [Abstract] [Full Text] [PDF]

				P. Fanara, J. Banerjee, R. V. Hueck, M. R. Harper, M. Awada, H. Turner, K. H. Husted, R. Brandt, and M. K. Hellerstein Stabilization of Hyperdynamic Microtubules Is Neuroprotective in Amyotrophic Lateral Sclerosis J. Biol. Chem., August 10, 2007; 282(32): 23465 - 23472. [Abstract] [Full Text] [PDF]

				M. Escobar-Khondiker, M. Hollerhage, M.-P. Muriel, P. Champy, A. Bach, C. Depienne, G. Respondek, E. S. Yamada, A. Lannuzel, T. Yagi, et al. Annonacin, a Natural Mitochondrial Complex I Inhibitor, Causes Tau Pathology in Cultured Neurons J. Neurosci., July 18, 2007; 27(29): 7827 - 7837. [Abstract] [Full Text] [PDF]

				M. Cyrklaff, M. Kudryashev, A. Leis, K. Leonard, W. Baumeister, R. Menard, M. Meissner, and F. Frischknecht Cryoelectron tomography reveals periodic material at the inner side of subpellicular microtubules in apicomplexan parasites J. Exp. Med., June 11, 2007; 204(6): 1281 - 1287. [Abstract] [Full Text] [PDF]

				J.-Z. Yu and M. M. Rasenick Tau associates with actin in differentiating PC12 cells FASEB J, July 1, 2006; 20(9): 1452 - 1461. [Abstract] [Full Text] [PDF]