Document Detail


Proteome identification of binding-partners interacting with cell polarity protein Par3 in Jurkat cells.
MedLine Citation:
PMID:  18685789     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The evolutionarily conserved cell polarity protein Par3, a scaffold-like PDZ-containing protein, plays a critical role in the establishment and maintenance of epithelial cell polarity. Although the role of Par3 in establishing cell polarity in epithelial cells has been intensively explored, the function of Par3 in hematopoietic cells remains elusive. To address this issue, we generated GST-fusion proteins of Par3 PDZ domains. By combining the GST-pull-down approach with liquid chromatography-tandem mass spectrometry, we identified 10 potential novel binding proteins of PDZ domains of Par3 in Jurkat cells (a T-cell line). The interaction of Par3 with three proteins--nuclear transport protein importin-alpha4 and proteasome activators PA28beta and PA28gamma--was confirmed using in vitro binding assay, co-immunoprecipitation assay and immunofluorescence microscopy. Our results have the potential to uncover novel functions of the cell polarity protein Par3 in blood cells.
Authors:
Ying Zhou; Longhou Fang; Dan Du; Wenchao Zhou; Xiujing Feng; Jiwu Chen; Zhe Zhang; Zhengjun Chen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Acta biochimica et biophysica Sinica     Volume:  40     ISSN:  1745-7270     ISO Abbreviation:  Acta Biochim. Biophys. Sin. (Shanghai)     Publication Date:  2008 Aug 
Date Detail:
Created Date:  2008-08-07     Completed Date:  2008-09-30     Revised Date:  2011-01-07    
Medline Journal Info:
Nlm Unique ID:  101206716     Medline TA:  Acta Biochim Biophys Sin (Shanghai)     Country:  China    
Other Details:
Languages:  eng     Pagination:  729-39     Citation Subset:  IM    
Affiliation:
School of Life Science, East China Normal University, Shanghai 200062, China.
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MeSH Terms
Descriptor/Qualifier:
Animals
Autoantigens / genetics,  metabolism
Base Sequence
Binding Sites
Cell Cycle Proteins / chemistry,  genetics,  metabolism*
Cell Line
Cell Polarity / physiology*
DNA Primers / genetics
Dogs
Humans
Jurkat Cells
Membrane Proteins / chemistry,  genetics,  metabolism*
Muscle Proteins / genetics,  metabolism
PDZ Domains
Proteasome Endopeptidase Complex / genetics,  metabolism
Protein Binding
Protein Interaction Domains and Motifs
Proteome / metabolism*
Recombinant Fusion Proteins / chemistry,  genetics,  metabolism
Transfection
alpha Karyopherins / genetics,  metabolism
Chemical
Reg. No./Substance:
0/Autoantigens; 0/Cell Cycle Proteins; 0/DNA Primers; 0/KPNA3 protein, human; 0/Ki antigen; 0/Membrane Proteins; 0/Muscle Proteins; 0/PARD3 protein, human; 0/Proteome; 0/Recombinant Fusion Proteins; 0/alpha Karyopherins; EC 3.4.25.1/PSME2 protein, human; EC 3.4.25.1/Proteasome Endopeptidase Complex

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


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