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First published online 22 February 2005
doi: 10.1242/jcs.01719

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

¹ Department of Biochemistry, New York University Medical Center, 550 First Avenue, New York, NY 10016, USA
² Department of Biological Sciences, Lehigh University, 111 Research Drive, Bethlehem, PA 18015, USA

^* Author for correspondence (e-mail: cowann01{at}endeavor.med.nyu.edu)

Accepted 11 January 2005

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.

Key words: Cofactor E, Tubulin, Microtubules, Tubulin stability

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