RGD Reference Report - Nephrin and Neph1 co-localize at the podocyte foot process intercellular junction and form cis hetero-oligomers. - Rat Genome Database

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Nephrin and Neph1 co-localize at the podocyte foot process intercellular junction and form cis hetero-oligomers.

Authors: Barletta, GM  Kovari, IA  Verma, RK  Kerjaschki, D  Holzman, LB 
Citation: Barletta GM, etal., J Biol Chem 2003 May 23;278(21):19266-71. Epub 2003 Mar 19.
RGD ID: 1299583
Pubmed: PMID:12646566   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M301279200   (Journal Full-text)

Glomerular visceral epithelial cells (podocytes) appear to play a central role in maintaining the selective filtration barrier of the renal glomerulus. While the immunoglobulin superfamily member Nephrin was proposed to act as a cell adhesion molecule at the podocyte intercellular junction necessary for maintaining glomerular perm selectivity, the Nephrin ligand has not been identified. The existence of a new subfamily of Nephrin-like molecules including Neph1 was recently described. Genetic deletion of Nephrin or Neph1 resulted in similar phenotypes of podocyte foot process effacement and proteinuria. The subcellular localization of Neph1 and the possibility that Nephrin and Neph1 interact was investigated. Polyclonal antiserum for Neph1 was raised and characterized. Neph1 migrated as a 90-kDa protein on SDS-PAGE under reducing conditions. Neph1 was identified in a glomerular and podocyte-specific distribution in adult rat kidney. Like Nephrin and Podocin, Neph1 was enriched in Triton X-100 detergent-resistant membrane fractions. Consistent with this observation, immunogold electron microscopy demonstrated that Neph1 localized exclusively to lateral margins of podocyte foot processes at the insertion of the slit diaphragm. Neph1 and Nephrin participate in a direct cis-interaction involving their cytoplasmic domains. In addition, interactions between the extracellular domain of Nephrin and itself and between the extracellular domain of Nephrin and that of Neph1 were detected. Neph1 did not interact via a homophilic interaction. These observations suggest that Nephrin and Neph1 form a hetero-oligomeric receptor complex in the plane of the membrane that might interact across the foot process intercellular junction through interactions between Nephrin with itself and Neph1.

Gene Ontology Annotations    Click to see Annotation Detail View

Cellular Component
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
cell projection membrane  IDA 1299583 RGD 
cell-cell junction  IDA 1299583 RGD 

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
protein binding  IPINphs1 (Rattus norvegicus)1299583 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Kirrel1  (kirre like nephrin family adhesion molecule 1)

Objects referenced in this article
Gene Nphs1 NPHS1 adhesion molecule, nephrin Rattus norvegicus

Additional Information