Document Detail

Trans-interaction of nephrin and Neph1/Neph3 induces cell adhesion that associates with decreased tyrosine phosphorylation of nephrin.
MedLine Citation:
PMID:  21306299     Owner:  NLM     Status:  Publisher    
Slit diaphragms are specialized junctions between glomerular epithelial cells (podocytes) that are crucial for glomerular ultrafiltration. Ig superfamily members nephrin and Neph1 are essential components of the slit diaphragm, whereas the role of Neph1 homologue Neph3 in the slit diaphragm is unknown. Here we show that Neph3 homodimerizes and heterodimerizes with nephrin and Neph1. We further investigated whether these interactions play a role in cell adhesion by using mouse L fibroblasts that lack endogenous cell adhesion activity, and found that Neph1 and Neph3 are able to induce cell adhesion alone whereas nephrin needs to trans-interact with Neph1 or Neph3 in order to promote formation of cell-cell contacts. Tyrosine phosphorylation of nephrin was down-regulated after nephrin trans-interacted with either Neph1 or Neph3 leading to formation of cell-cell contacts. We further found that the expression of Neph3 was increased in nephrin deficient mouse kidneys suggesting that Neph3 may participate in the formation of tight-junction-like structures observed in nephrin deficient podocytes. Our findings show that nephrin and Neph1 or Neph3 trans-interactions promote cell contact formation suggesting that they could function together also in the slit diaphragm assembly, and when nephrin is absent, participate in the formation of altered junctional complexes between podocyte foot processes.
Eija Heikkilä; Mervi Ristola; Marika Havana; Nina Jones; Harry Holthöfer; Sanna Lehtonen
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-2-9
Journal Detail:
Title:  The Biochemical journal     Volume:  -     ISSN:  1470-8728     ISO Abbreviation:  -     Publication Date:  2011 Feb 
Date Detail:
Created Date:  2011-2-10     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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