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JCS ePress online publication date 22 Feb 2005
doi: 10.1242/jcs.01719

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Research Article

Identification of a novel tubulin-destabilizing protein related to the chaperone cofactor E


Francesca Bartolini, Guoling Tian, Michelle Piehl, Lynne Cassimeris, Sally A. Lewis, and Nicholas J. Cowan*
* Author for correspondence (e-mail: cowann01{at}endeavor.med.nyu.edu)

Factors that regulate the microtubule cytoskeleton are critical in determining cell behavior. Here we describe the function of a novel protein that we term E-like based on its sequence similarity to the tubulin-specific chaperone cofactor E. We find that upon overexpression, E-like depolymerizes microtubules by committing tubulin to proteosomal degradation. Our data suggest that this function is direct and is based on the ability of E-like to disrupt the tubulin heterodimer in vitro. Suppression of E-like expression results in an increase in the number of stable microtubules and a tight clustering of endocellular membranes around the microtubule-organizing center, while the properties of dynamic microtubules are unaffected. These observations define E-like as a novel regulator of tubulin stability, and provide a link between tubulin turnover and vesicle transport.
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