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Distinct distribution of specific members of protein 4.1 gene family in the mouse nephron.

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TLDR
Distinct distribution of 4.1 proteins along the nephron suggests their involvement in targeting of selected transmembrane proteins in kidney epithelium and, therefore, in regulation of specific kidney functions.
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This article is published in Kidney International.The article was published on 2003-04-01 and is currently open access. It has received 56 citations till now. The article focuses on the topics: Distal convoluted tubule & Nephron.

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Citations
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Organization of the pronephric filtration apparatus in zebrafish requires Nephrin, Podocin and the FERM domain protein Mosaic eyes.

TL;DR: A functional assay of glomerular filtration barrier revealed that absence of normal nephrin, podocin or mosaic eyes expression results in loss ofglomerularfiltration discrimination and aberrant passage of high molecular weight substances into the glomersular filtrate.
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Fox-2 Splicing Factor Binds to a Conserved Intron Motif to Promote Inclusion of Protein 4.1R Alternative Exon 16

TL;DR: It is demonstrated that positive regulation of E16 splicing can be mediated by Fox-2 or Fox-1, two closely related splicing factors that possess identical RNA recognition motifs, and proposed that the Fox family of splicing enhancers plays an important role in alternative splicing switches during differentiation in metazoan organisms.
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The spectrin–ankyrin–4.1–adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life

TL;DR: The spectrin–ankyrin–4.1–adducin complex represents a remarkable system that underpins animal life; it has been adapted to many different functions at different times during animal evolution.
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The Protein 4.1 family: hub proteins in animals for organizing membrane proteins.

TL;DR: It is hypothesized that differential regulation of 4.1 proteins and ankyrins allows highly selective control of cell surface protein accumulation and, hence, function.
References
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Journal ArticleDOI

Biochemical Analysis of Potential Sites for Protein 4.1-mediated Anchoring of the Spectrin-Actin Skeleton to the Erythrocyte Membrane

TL;DR: It is shown that proteolytic removal of the cytoplasmic domain of band 3 has minimal effect on the ability of protein 4.1 to promote125I-labeled spectrin and actin binding to KI-stripped erythrocyte membrane vesicles, and band 3 is incapable of serving the same function.
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Distribution of cell membrane-associated proteins along the human nephron.

TL;DR: A histochemical analysis of the distribution of proteins associated with specific cell adhesion complexes and membrane proteins in biopsy specimens of human kidney taken from healthy kidney transplant donors found each protein to have a characteristic subcellular localization and an intensity of staining that varied among different segments of the nephron in a manner that is consistent with discrete, segmental nephrons function.
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Cytoskeleton-membrane connections in the human erythrocyte membrane: band 4.1 binds to tetrameric band 3 protein.

TL;DR: The results described, together with those reported previously, point at a prominent role of tetrameric band 3 in ligand binding, at low molar ratios of band 4.1 and band 3.
Journal Article

Terminal differentiation in epithelia: the Hensin pathway in intercalated cells.

TL;DR: All of these studies show that the conversion of polarity in the intercalated cell, at least in vitro, represents terminal differentiation and that hensin is the first protein in a new pathway that mediates this process.
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NHE3 activity and trafficking depend on the state of actin organization in proximal tubule.

TL;DR: NHE3 activity depends on the state of actin organization possibly involved in trafficking processes between luminal membrane and intracellular compartment under basal conditions, and on the effect of Cyto D on NHE3.
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