Document Detail

XMAP215 regulates microtubule dynamics through two distinct domains.
MedLine Citation:
PMID:  11157747     Owner:  NLM     Status:  MEDLINE    
XMAP215 belongs to a family of proteins involved in the regulation of microtubule dynamics. In this study we analyze the function of different parts of XMAP215 in vivo and in Xenopus egg extracts. XMAP215 has been divided into three fragments, FrN, FrM and FrC (for N-terminal, middle and C-terminal, respectively). FrN co-localizes with microtubules in egg extracts but not in cells, FrC co- localizes with microtubules and centrosomes both in egg extracts and in cells, while FrM does not co- localize with either centrosomes or microtubules. In Xenopus egg extracts, FrN stimulates microtubule growth at plus-ends by inhibiting catastrophes, while FrM has no effect, and FrC suppresses microtubule growth by promoting catastrophes. Our results suggest that XMAP215 is targeted to centrosomes and microtubules mainly through its C-terminal domain, while the evolutionarily conserved N-terminal domain contains its microtubule-stabilizing activity.
A V Popov; A Pozniakovsky; I Arnal; C Antony; A J Ashford; K Kinoshita; R Tournebize; A A Hyman; E Karsenti
Related Documents :
19759037 - Social learning about egg-laying substrates in fruitflies.
19041117 - Mycotoxin analyses in some home produced eggs in belgium reveal small contribution to t...
17969607 - Shell egg handling and preparation practices in food service establishments in finland.
8245947 - Oviposition response of aedes aegypti mosquitoes to different concentrations of hay inf...
17224467 - Genetic evaluation of beef carcass data using different endpoint adjustments.
4752087 - The form of the auto-shaped response with food or water reinforcers.
Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The EMBO journal     Volume:  20     ISSN:  0261-4189     ISO Abbreviation:  EMBO J.     Publication Date:  2001 Feb 
Date Detail:
Created Date:  2001-02-22     Completed Date:  2001-03-22     Revised Date:  2013-04-18    
Medline Journal Info:
Nlm Unique ID:  8208664     Medline TA:  EMBO J     Country:  England    
Other Details:
Languages:  eng     Pagination:  397-410     Citation Subset:  IM    
Cell Biology Program, EMBL, Meyerhofstrasse 1, Heidelberg 69117, Germany.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Binding Sites
Cell Line
Centrosome / metabolism,  ultrastructure
Microscopy, Immunoelectron
Microtubule-Associated Proteins / chemistry*,  genetics,  metabolism*
Microtubules / metabolism*,  ultrastructure
Oocytes / metabolism
Peptide Fragments / chemistry,  genetics,  metabolism
Protein Structure, Tertiary
Xenopus Proteins*
Reg. No./Substance:
0/Microtubule-Associated Proteins; 0/Peptide Fragments; 0/XMAP215 protein, Xenopus; 0/Xenopus Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  The human cytomegalovirus gene product US6 inhibits ATP binding by TAP.
Next Document:  t-SNARE dephosphorylation promotes SNARE assembly and exocytosis in yeast.