ArticleMolecular and cellular biology2012
CD2AP regulates SUMOylation of CIN85 in podocytes.
Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
- Advances in SRNS Gene Research: From Precision Classification to Precision Diagnosis and Treatment.Biomedicines · 2026Review
- Fundamental Processes in Renal Function Discovered at the Mt. Desert Island Biological Laboratory.Kidney360 · 2026Review
- Article
- The Life of a Kidney Podocyte.Acta physiologica (Oxford, England) · 2025Review
- Noncanonical function of folate through folate receptor 1 during neural tube formation.Nature communications · 2024Article
- Exploring potential targets for natural product therapy of DN: the role of SUMOylation.Frontiers in pharmacology · 2024Review
- Natural Products Against Renal FibrosisFrontiers in pharmacology · 2022Review
- Endocytic Trafficking at the Mature Podocyte Slit Diaphragm.Frontiers in pediatrics · 2017Review
- Bin1 and CD2AP polarise the endocytic generation of beta-amyloid.EMBO reports · 2017Article
- Podocin is translocated to cytoplasm in puromycin aminonucleoside nephrosis rats and in poor-prognosis patients with IgA nephropathy.Cell and tissue research · 2015Article
- ARAP3 functions in hematopoietic stem cells.PloS one · 2014Article
- Membrane trafficking in podocyte health and disease.Pediatric nephrology (Berlin, Germany) · 2013Review
- The function of endocytosis in podocytes.Current opinion in nephrology and hypertension · 2013Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Podocytes are highly differentiated and polarized epithelial cells located on the visceral side of the glomerulus. They form an indispensable component of the glomerular filter, the slit diaphragm, formed by several transmembrane proteins and adaptor molecules. Disruption of the slit diaphragm can lead to massive proteinuria and nephrotic syndrome in mice and humans. CD2AP is an adaptor protein that is important for the maintenance of the slit diaphragm. Together with its paralogue, CIN85, CD2AP belongs to a family of adaptor proteins that are primarily described as being involved in endocytosis and downregulation of receptor tyrosine kinase activity. We have shown that full-length CIN85 is upregulated in podocytes in the absence of CD2AP, whereas in wild-type cells, full-length CIN85 is not detectable. In this study, we show that full-length CIN85 is postranslationally modified by SUMOylation in wild-type podocytes. We can demonstrate that CIN85 is SUMOylated by SUMO-1, -2, and -3 and that SUMOylation is enhanced in the presence of CD2AP. Conversion of lysine 598 to arginine completely abolishes SUMOylation and leads to increased binding of CIN85 to nephrin. Our results indicate a novel role for CD2AP in regulating posttranslational modification of CIN85.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.