Podocin, a raft-associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrin.

@article{Schwarz2001PodocinAR,
  title={Podocin, a raft-associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrin.},
  author={K Schwarz and Matias Simons and Jochen Reiser and Moin A. Saleem and Christian Faul and Wilhelm Kriz and Andrey S. Shaw and Lawrence B. Holzman and Peter Mundel},
  journal={The Journal of clinical investigation},
  year={2001},
  volume={108 11},
  pages={
          1621-9
        }
}
NPHS2 was recently identified as a gene whose mutations cause autosomal recessive steroid-resistant nephrotic syndrome. Its product, podocin, is a new member of the stomatin family, which consists of hairpin-like integral membrane proteins with intracellular NH(2)- and COOH-termini. Podocin is expressed in glomerular podocytes, but its subcellular distribution and interaction with other proteins are unknown. Here we show, by immunoelectron microscopy, that podocin localizes to the podocyte foot… Expand
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TLDR
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TLDR
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TLDR
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Structural features and oligomeric nature of human podocin domain
TLDR
It is shown that the podocin domain majorly homo-oligomerizes into a 16-mer oligomer, and Circular dichroism and fluorescence spectroscopy suggest that the 16-MER oligomer has considerable secondary structure and moderate tertiary packing. Expand
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References

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TLDR
It is suggested that lipid rafts are important in the spatial organization of the glomerular slit diaphragm under physiological and pathological conditions. Expand
CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain.
TLDR
It is demonstrated thatCD2AP localizes to the slit diaphragm in podocytes using immunoelectron microscopy and that nephrin and CD2AP co-immunoprecipitate from a podocyte cell line, lending further support to the idea that CD2 AP plays a role in the structural integrity of the slitDiaphragms. Expand
Interaction with Podocin Facilitates Nephrin Signaling*
TLDR
It is demonstrated now that nephrin is a signaling molecule, which stimulates mitogen-activated protein kinases, which enhances Nephrin-induced signaling is greatly enhanced by podocin, which binds to the cytoplasmic tail of nephin. Expand
Nephrin is specifically located at the slit diaphragm of glomerular podocytes.
TLDR
The size and location of nephrin, the first protein to be identified at the glomerular podocyte slit diaphragm area, are described and an essential role for this protein in the normal glomersular filtration barrier is suggested. Expand
Nephrin localizes to the slit pore of the glomerular epithelial cell.
TLDR
As a putative cell adhesion molecule of the immunoglobulin superfamily, nephrin likely participates in cell-cell interactions between podocyte foot processes and may represent a component of the slit diaphragm. Expand
CD2AP is expressed with nephrin in developing podocytes and is found widely in mature kidney and elsewhere.
TLDR
Results suggest that CD2AP is not only involved in maintaining the slit diaphragm but may also have a general role in maintaining specialized subcellular architecture. Expand
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TLDR
The molecular structure of FAT and its colocalization with 5-1-6 antigen and ZO-1 indicate that FAT is a component of slit diaphragms. Expand
Nephrin localizes at the podocyte filtration slit area and is characteristically spliced in the human kidney.
TLDR
Results indicate that nephrin is a new protein of the interpodocyte filtration slit area with a profound role in the pathophysiology of the filTration barrier. Expand
The glomerular slit diaphragm is a modified adherens junction.
TLDR
A P-cadherin-based adherens junction is well-suited to explain the zipper-like structure of the slit diaphragm, and the present study should allow new avenues leading to the identification of additional slit diphragm-associated proteins conferring specificity to this unique cell junction. Expand
NPHS2, encoding the glomerular protein podocin, is mutated in autosomal recessive steroid-resistant nephrotic syndrome
TLDR
It is found that ten different NPHS2 mutations, comprising nonsense, frameshift and missense mutations, to segregate with the disease, demonstrating a crucial role for podocin in the function of the glomerular filtration barrier. Expand
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