Document Detail


Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex.
MedLine Citation:
PMID:  12221128     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Microtubule assembly is initiated by the gamma-tubulin ring complex (gamma-TuRC). In yeast, the microtubule is nucleated from gamma-TuRC anchored to the amino-terminus of the spindle pole body component Spc110p, which interacts with calmodulin (Cmd1p) at the carboxy-terminus. However, mammalian protein that anchors gamma-TuRC remains to be elucidated. A giant coiled-coil protein, CG-NAP (centrosome and Golgi localized PKN-associated protein), was localized to the centrosome via the carboxyl-terminal region. This region was found to interact with calmodulin by yeast two-hybrid screening, and it shares high homology with the carboxyl-terminal region of another centrosomal coiled-coil protein, kendrin. The amino-terminal region of either CG-NAP or kendrin indirectly associated with gamma-tubulin through binding with gamma-tubulin complex protein 2 (GCP2) and/or GCP3. Furthermore, endogenous CG-NAP and kendrin were coimmunoprecipitated with each other and with endogenous GCP2 and gamma-tubulin, suggesting that CG-NAP and kendrin form complexes and interact with gamma-TuRC in vivo. These proteins were localized to the center of microtubule asters nucleated from isolated centrosomes. Pretreatment of the centrosomes by antibody to CG-NAP or kendrin moderately inhibited the microtubule nucleation; moreover, the combination of these antibodies resulted in stronger inhibition. These results imply that CG-NAP and kendrin provide sites for microtubule nucleation in the mammalian centrosome by anchoring gamma-TuRC.
Authors:
Mikiko Takahashi; Akiko Yamagiwa; Tamako Nishimura; Hideyuki Mukai; Yoshitaka Ono
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular biology of the cell     Volume:  13     ISSN:  1059-1524     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2002 Sep 
Date Detail:
Created Date:  2002-09-10     Completed Date:  2003-03-12     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3235-45     Citation Subset:  IM    
Affiliation:
Biosignal Research Center, Kobe University, Japan.
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MeSH Terms
Descriptor/Qualifier:
A Kinase Anchor Proteins
Adaptor Proteins, Signal Transducing*
Amino Acid Sequence
Animals
CHO Cells
COS Cells
Calmodulin-Binding Proteins / metabolism*
Carrier Proteins / metabolism*
Cell Line
Cell Nucleus / metabolism*
Centrosome / metabolism
Cricetinae
Cytoskeletal Proteins*
DNA, Complementary / metabolism
Hela Cells
Humans
Immunoblotting
Microscopy, Fluorescence
Microtubule-Associated Proteins / metabolism
Microtubules / metabolism*,  ultrastructure
Models, Genetic
Molecular Sequence Data
Precipitin Tests
Protein Binding
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Transfection
Tubulin / metabolism*
Two-Hybrid System Techniques
Chemical
Reg. No./Substance:
0/A Kinase Anchor Proteins; 0/AKAP9 protein, human; 0/Adaptor Proteins, Signal Transducing; 0/Calmodulin-Binding Proteins; 0/Carrier Proteins; 0/Cytoskeletal Proteins; 0/DNA, Complementary; 0/Microtubule-Associated Proteins; 0/TUBGCP2 protein, human; 0/TUBGCP3 protein, human; 0/Tubulin; 0/kendrin
Comments/Corrections

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


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