spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

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

Journal of Cell Science 118, 1197-1207 (2005)
Published by The Company of Biologists 2005
This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
jcs.01719v1
118/6/1197    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Related articles in JCS
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bartolini, F.
Right arrow Articles by Cowan, N. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bartolini, F.
Right arrow Articles by Cowan, N. J.

Research Article

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

Francesca Bartolini1, Guoling Tian1, Michelle Piehl2, Lynne Cassimeris2, Sally A. Lewis1 and Nicholas J. Cowan1,*

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


Related articles in JCS:

Microtubules down the tube

JCS 2005 118: 601. [Full Text]  





© The Company of Biologists Ltd 2005