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Updated: Jul 9, 2026

Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence (TIRF) Microscopy
Published on: July 20, 2022
Measurements of stathmin-tubulin interaction in solution
1Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Gif-sur-Yvette, France.
Abstract:
Stathmin is an important phosphorylation-controlled regulator of microtubule dynamics and plays a crucial role in cell division and cell proliferation. In its non-phosphorylated form, stathmin is the protein that interacts the most tightly with tubulin, in a 2:1 tubulin-stathmin (T2S) complex that does not participate in microtubule assembly. The importance of stathmin at different levels of phosphorylation in different steps of mitosis This article is a short overview of the different methods that have been or could be used to monitor the kinetic and thermodynamic parameters of tubulin-stathmin interaction and to evaluate the effects of phosphorylation. The author has tried to emphasize how hydrodynamic and spectroscopic methods measuring direct binding of stathmin to tubulin can be complemented by methods that make use of linked functions, measuring how the change in a functional property of tubulin upon binding stathmin provides information on binding parameters.

