Document Detail

Densin and beta-catenin form a complex and co-localize in cultured podocyte cell junctions.
MedLine Citation:
PMID:  17581699     Owner:  NLM     Status:  MEDLINE    
Densin is a member of LAP (leucine-rich repeat and PDZ domain) protein family that localizes in kidney to slit diaphragms, which are essential components of the glomerular filtration barrier. We have previously shown that densin interacts with a crucial slit diaphragm protein, nephrin. Here, we searched for novel binding partners of densin by yeast-two hybrid assay and identified beta-catenin. The interaction was confirmed by reciprocal co-immunoprecipitation assay and the binding site in densin was determined by GST-pull down assays. The GST-tagged densin was also able to pull down P-cadherin together with beta-catenin from human kidney glomerular lysates. Furthermore, densin co-localized with beta-catenin and F-actin in cell-cell contacts in cultured mouse podocytes. During cell-cell contact disruption and reformation densin and beta-catenin were dislocated from and relocated back to plasma membrane in a similar fashion. These and our previous findings suggest that densin may associate with the cadherin-catenin and nephrin complex(es), and may be involved in the formation of the cell-cell contacts including the slit diaphragm.
Eija Heikkilä; Mervi Ristola; Karlhans Endlich; Sanna Lehtonen; Markus Lassila; Marika Havana; Nicole Endlich; Harry Holthöfer;
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-06-21
Journal Detail:
Title:  Molecular and cellular biochemistry     Volume:  305     ISSN:  0300-8177     ISO Abbreviation:  Mol. Cell. Biochem.     Publication Date:  2007 Nov 
Date Detail:
Created Date:  2007-10-02     Completed Date:  2007-12-07     Revised Date:  2007-12-17    
Medline Journal Info:
Nlm Unique ID:  0364456     Medline TA:  Mol Cell Biochem     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  9-18     Citation Subset:  IM    
Department of Bacteriology and Immunology, Haartman Institute, University of Helsinki, Helsinki, Finland.
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MeSH Terms
Binding Sites
Cadherins / metabolism
Calcium / metabolism
Cells, Cultured
Intercellular Junctions / metabolism*
Membrane Proteins / metabolism
Multiprotein Complexes / metabolism
Podocytes / metabolism*
Protein Binding / drug effects
Protein Interaction Mapping
Puromycin Aminonucleoside / pharmacology
Recombinant Fusion Proteins / metabolism
Sialoglycoproteins / metabolism*
Tissue Distribution
beta Catenin / metabolism*
Reg. No./Substance:
0/Cadherins; 0/LRRC7 protein, human; 0/Membrane Proteins; 0/Multiprotein Complexes; 0/Recombinant Fusion Proteins; 0/Sialoglycoproteins; 0/beta Catenin; 0/nephrin; 58-60-6/Puromycin Aminonucleoside; 7440-70-2/Calcium

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

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