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MAGI-2 orchestrates the localization of backbone proteins in the slit diaphragm of podocytes.

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TLDR
The role of membrane-associated guanylate kinase inverted 2 (MAGI-2) is focused on in order to investigate mechanisms that orchestrate localization of slit-diaphragm backbone proteins in podocytes and to elucidate a mechanism by which the backbone proteins are maintained.
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This article is published in Kidney International.The article was published on 2021-02-01 and is currently open access. It has received 14 citations till now. The article focuses on the topics: Nephrin & Podocyte.

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Intestinal Bacterial Translocation Contributes to Diabetic Kidney Disease

TL;DR: In this paper , the effects of disrupted intestinal homeostasis associated with Mitochondrial antiviral signaling protein (MAVS), a component of innate immunity, maintains intestinal integrity was investigated in diabetic kidney disease.
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Mapping the human kidney using single-cell genomics

TL;DR: The state of the art of single-cell analyses in kidney research is summarized, including advances in the understanding of kidney embryogenesis and pathomechanisms of several relevant kidney disease entities.
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MAGI1, a Scaffold Protein with Tumor Suppressive and Vascular Functions.

TL;DR: MAGI1 is a cytoplasmic scaffolding protein initially identified as a component of cell-to-cell contacts stabilizing cadherin-mediated cell-cell adhesion in epithelial and endothelial cells.
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Proximity proteomics of synaptopodin provides insight into the molecular composition of the spine apparatus of dendritic spines

TL;DR: Using an in vivo spatial proteomics technique, this work identifies proteins associated with the spine apparatus and validate the specific localization of a subset of them, including Pdlim7, in neurons, allowing for better understanding of brain function in health and disease.
References
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Journal ArticleDOI

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

TL;DR: It is shown, by immunoelectron microscopy, that podocin localizes to the podocyte foot process membrane, at the insertion site of the slit diaphragm, and it is postulate thatpodocin serves in the structural organization of the slat diaphagm and the regulation of its filtration function.
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Proteinuria and perinatal lethality in mice lacking NEPH1, a novel protein with homology to NEPHRIN.

TL;DR: Findings suggest that NEPH1, like NEPHRIN, may play an important role in maintaining the structure of the filtration barrier that prevents proteins from freely entering the glomerular urinary space.
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A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins.

TL;DR: A yeast two-hybrid screening for SAPAP-interacting molecules is performed and a novel protein is identified that has an inverse structure of membrane-associated guanylate kinases with an NH2-terminal GK-like domain followed by two WW and five PDZ domains called S-SCAM (synaptic scaffolding molecule), which may assemble receptors and cell adhesion proteins at synaptic junctions.
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CD2AP Localizes to the Slit Diaphragm and Binds to Nephrin via a Novel C-Terminal Domain

TL;DR: 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.
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