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Microtubule Structural Dynamics Measured with Impedance Spectroscopy
Author(s) -
Whittier Jennifer E.,
Goddard Greg R
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a492-b
Subject(s) - microtubule , tubulin , biophysics , microtubule polymerization , cytoskeleton , chemistry , microbiology and biotechnology , biology , cell , biochemistry
Microtubules are ubiquitous cytoskeletal proteins that play an important role in a variety of cellular processes. It has been demonstrated that microtubules are essential components in cellular activities as diverse as mitotic spindle formation, dendrite outgrowth at synapses, and vesicle transport. In vivo , these proteins exist in a constant state of dynamic instability, alternating between the polymerized microtubule and depolymerized tubulin subunits. Due to this property, very little is known about the dynamic structural features of microtubules. We use impedance spectroscopy to study structural details of microtubules, probing polymerization and binding events in nearly real time without the need for optically active labels. Using this method, we have obtained data for polymerization rates and microtubule‐associated protein 2 (MAP2) and tau binding that agree with previously published results. Additionally, we can distinguish the presence of multiple conduction pathways along the microtubule, which correspond to the presence of various isoforms of tubulin present in the sample. Finally, we look at single neuronal cells in an attempt to monitor microtubule behavior in vivo. We then discuss the greater applicability of this technique in the biological sciences.