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Article

CIN85/RukL Is a Novel Binding Partner of Nephrin and Podocin and Mediates Slit Diaphragm Turnover in Podocytes

11 May 2010

Abstract excerpt

Podocyte damage is the basis of many glomerular diseases with ultrastructural changes and decreased expression of components of the slit diaphragm such as nephrin and podocin. Under physiological conditions it is likely that the slit diaphragm underlies permanent renewal processes to indemnify its stability in response to changes in filtration pressure. This would require constant reorganization of the podocyte...

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Share to Biomedical Research and Pathophysiology
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Identifiers

PMID: 20457601
DOI: 10.1074/jbc.m109.087239

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Related research

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Research trail→

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CIN85/RukL Is a Novel Binding Partner of Nephrin and Podocin and Mediates Slit Diaphragm Turnover in PodocytesPMID 20457601Read ↗

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An update: the role of Nephrin inside and outside the kidneySemantic proximity Read ↗

Nephrin-signature molecule of the glomerular podocyte?Semantic proximity Read ↗

Multiple domains of Ruk/CIN85/SETA/CD2BP3 are involved in interaction with p85alpha regulatory subunit of PI 3-kinase.Semantic proximity Read ↗

The ubiquitin ligase Ubr4 controls stability of podocin/MEC-2 supercomplexesSemantic proximity Read ↗

Selective endocytosis controls slit diaphragm maintenance and dynamicsSemantic proximity Read ↗

CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain.Semantic proximity Read ↗

Interaction with Podocin Facilitates Nephrin SignalingSemantic proximity Read ↗

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