{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10"],"submitter":["Maywald ML"],"pubmed_abstract":["Glomerular podocytes build, with their intercellular junctions, part of the kidney filter. The podocyte cell adhesion protein, nephrin, is essential for developing and maintaining slit diaphragms as functional loss in humans results in heavy proteinuria. Nephrin expression and function are also altered in many adult-onset glomerulopathies. Nephrin signals from the slit diaphragm to the actin cytoskeleton and integrin β1 at focal adhesions by recruiting Crk family proteins, which can interact with the Rap guanine nucleotide exchange factor 1 C3G. As Rap1 activity affects focal adhesion formation, we hypothesize that nephrin signals <i>via</i> Rap1 to integrin β. To address this issue, we combined <i>Drosophila in vivo</i> and mammalian cell culture experiments. We find that Rap1 is necessar"],"journal":["Frontiers in cell and developmental biology"],"pagination":["790365"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8972170"],"repository":["biostudies-literature"],"pubmed_title":["Rap1 Activity Is Essential for Focal Adhesion and Slit Diaphragm Integrity."],"pmcid":["PMC8972170"],"pubmed_authors":["Picciotto C","Pavenstadt H","Krahn MP","Maywald ML","Klingauf J","George B","Bertgen L","Ricker A","Yousaf FS","Lepa C"],"additional_accession":[]},"is_claimable":false,"name":"Rap1 Activity Is Essential for Focal Adhesion and Slit Diaphragm Integrity.","description":"Glomerular podocytes build, with their intercellular junctions, part of the kidney filter. The podocyte cell adhesion protein, nephrin, is essential for developing and maintaining slit diaphragms as functional loss in humans results in heavy proteinuria. Nephrin expression and function are also altered in many adult-onset glomerulopathies. Nephrin signals from the slit diaphragm to the actin cytoskeleton and integrin β1 at focal adhesions by recruiting Crk family proteins, which can interact with the Rap guanine nucleotide exchange factor 1 C3G. As Rap1 activity affects focal adhesion formation, we hypothesize that nephrin signals <i>via</i> Rap1 to integrin β. To address this issue, we combined <i>Drosophila in vivo</i> and mammalian cell culture experiments. We find that Rap1 is necessar","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2025-04-22T07:49:49.731Z","creation":"2025-04-05T22:18:22.218Z"},"accession":"S-EPMC8972170","cross_references":{"pubmed":["35372328"],"doi":["10.3389/fcell.2022.790365"]}}