JCB logo
MBL International Tel: 800.200.5459 CLICK HERE
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online 5 September 2006. doi:10.1083/jcb.200512058
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 174, Number 6, 839-849
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 2828K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Peris, L.
Right arrow Articles by Job, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Peris, L.
Right arrow Articles by Job, D.
Right arrowPubmed/NCBI databases
*Gene*GEO Profiles
*HomoloGene*Nucleotide
*Protein*UniGene
*Compound via MeSH
*Substance via MeSH
Hazardous Substances DB
*L-TYROSINE
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Article

 Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends

Leticia Peris1, Manuel Thery2, Julien Fauré1, Yasmina Saoudi1, Laurence Lafanechère1, John K. Chilton3, Phillip Gordon-Weeks3, Niels Galjart4, Michel Bornens2, Linda Wordeman5, Juergen Wehland6, Annie Andrieux1, and Didier Job1

1 Laboratoire du Cytosquelette, Institut National de la Santé et de la Recherche Médicale U366, Département Réponse et Dynamique Cellulaire, Commisariat à l'Energie Atomique Grenoble, 38054 Grenoble, France
2 Biologie du Cycle Cellulaire et de la Motilité, UMR144, Centre National de la Recherche Scientifique, Institut Curie, 75248 Paris, Cedex 05, France
3 Medical Research Council Centre for Developmental Neurobiology, King's College London, London SE1 1UL, England, UK
4 Department of Cell Biology and Genetics, Erasmus Medical Center, 3000 DR Rotterdam, Netherlands
5 Department of Physiology and Biophysics, University of Washington, Seattle, WA 98195
6 Department of Cell Biology, German Research Center for Biotechnology, D-38124 Braunschweig, Germany

Correspondence to Didier Job: didier.job{at}cea.fr

Tubulin-tyrosine ligase (TTL), the enzyme that catalyzes the addition of a C-terminal tyrosine residue to {alpha}-tubulin in the tubulin tyrosination cycle, is involved in tumor progression and has a vital role in neuronal organization. We show that in mammalian fibroblasts, cytoplasmic linker protein (CLIP) 170 and other microtubule plus-end tracking proteins comprising a cytoskeleton-associated protein glycine-rich (CAP-Gly) microtubule binding domain such as CLIP-115 and p150 Glued, localize to the ends of tyrosinated microtubules but not to the ends of detyrosinated microtubules. In vitro, the head domains of CLIP-170 and of p150 Glued bind more efficiently to tyrosinated microtubules than to detyrosinated polymers. In TTL-null fibroblasts, tubulin detyrosination and CAP-Gly protein mislocalization correlate with defects in both spindle positioning during mitosis and cell morphology during interphase. These results indicate that tubulin tyrosination regulates microtubule interactions with CAP-Gly microtubule plus-end tracking proteins and provide explanations for the involvement of TTL in tumor progression and in neuronal organization.

Abbreviations used in this paper: CAP-Gly, cytoskeleton-associated protein glycine-rich; CLASP, CLIP-associating protein; CLIP, cytoplasmic linker protein; HD, head domain; MCAK, mitotic centromere-associated kinesin; MEF, mouse embryonic fibroblast; MT, microtubule; TTL, tubulin-tyrosine ligase; TCP, tubulin carboxypeptidase; WT, wild type.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents