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

Author:

Bartolini Francesca1,Tian Guoling1,Piehl Michelle2,Cassimeris Lynne2,Lewis Sally A.1,Cowan Nicholas J.1

Affiliation:

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

Abstract

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.

Publisher

The Company of Biologists

Subject

Cell Biology

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