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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

NEPH1 defines a novel family of podocin interacting proteins.

Mutations of NPHS1 or NPHS2, the genes encoding for the glomerular podocyte proteins nephrin and podocin, cause steroid-resistant proteinuria. In addition, mice lacking NEPH1 develop a nephrotic syndrome that resembles NPHS mutations, suggesting that all three proteins are essential for the integrity of glomerular podocytes. Podocin interacts with the C-terminal domain of nephrin and facilitates nephrin-dependent signaling. NEPH1, a member of the immunoglobulin superfamily, is structurally related to nephrin. We report now that NEPH1 belongs to a family of three closely related proteins that interact with the C-terminal domain of podocin. All three NEPH proteins share a conserved podocin-binding motif; mutation of a centrally located tyrosine residue dramatically lowers the affinity of NEPH1 for podocin. NEPH1 triggers AP-1 activation similarly to nephrin but requires the presence of Tec family kinases for efficient transactivation. We conclude that NEPH1 defines a new family of podocin- binding molecules that are potential candidates for hereditary nephrotic syndromes not linked to either NPHS1 or NPHS2.[1]


  1. NEPH1 defines a novel family of podocin interacting proteins. Sellin, L., Huber, T.B., Gerke, P., Quack, I., Pavenstädt, H., Walz, G. FASEB J. (2003) [Pubmed]
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