Document Detail

Crystal structure of γ-tubulin complex protein GCP4 provides insight into microtubule nucleation.
MedLine Citation:
PMID:  21725292     Owner:  NLM     Status:  MEDLINE    
Microtubule nucleation in all eukaryotes involves γ-tubulin small complexes (γTuSCs) that comprise two molecules of γ-tubulin bound to γ-tubulin complex proteins (GCPs) GCP2 and GCP3. In many eukaryotes, multiple γTuSCs associate with GCP4, GCP5 and GCP6 into large γ-tubulin ring complexes (γTuRCs). Recent cryo-EM studies indicate that a scaffold similar to γTuRCs is formed by lateral association of γTuSCs, with the C-terminal regions of GCP2 and GCP3 binding γ-tubulin molecules. However, the exact role of GCPs in microtubule nucleation remains unknown. Here we report the crystal structure of human GCP4 and show that its C-terminal domain binds directly to γ-tubulin. The human GCP4 structure is the prototype for all GCPs, as it can be precisely positioned within the γTuSC envelope, revealing the nature of protein-protein interactions and conformational changes regulating nucleation activity.
Valérie Guillet; Martine Knibiehler; Lynn Gregory-Pauron; Marie-Hélène Remy; Cécile Chemin; Brigitte Raynaud-Messina; Cécile Bon; Justin M Kollman; David A Agard; Andreas Merdes; Lionel Mourey
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2011-07-03
Journal Detail:
Title:  Nature structural & molecular biology     Volume:  18     ISSN:  1545-9985     ISO Abbreviation:  Nat. Struct. Mol. Biol.     Publication Date:  2011 Aug 
Date Detail:
Created Date:  2011-08-03     Completed Date:  2011-11-28     Revised Date:  2013-07-18    
Medline Journal Info:
Nlm Unique ID:  101186374     Medline TA:  Nat Struct Mol Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  915-9     Citation Subset:  IM    
Institut de Pharmacologie et de Biologie Structurale, Centre National de la Recherche Scientifique, Toulouse, France.
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MeSH Terms
Binding Sites
Crystallography, X-Ray
Microtubule-Associated Proteins / chemistry*,  physiology
Microtubules / metabolism*
Protein Interaction Domains and Motifs
Protein Structure, Tertiary
Tubulin / metabolism
Grant Support
GM31627/GM/NIGMS NIH HHS; R01 GM031627/GM/NIGMS NIH HHS; //Howard Hughes Medical Institute
Reg. No./Substance:
0/Microtubule-Associated Proteins; 0/TUBGCP4 protein, human; 0/Tubulin

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