Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells.

Morrow, Jon S.; Cianci, Carol D.; Ardito, Thomas; Mann, A. S.; Kashgarian, Michael

doi:10.1083/jcb.108.2.455

Cited by 263 publications

(117 citation statements)

References 53 publications

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“…A role for basolateral ankyrin-fodrin in facilitating Na,K-ATPase basolateral localization has been suggested in MDCK and renal tubule cells. 123,124 Conversely, ankyrin and fodrin were both found at the apical surface of choroid plexus and RPE cells, where ankyrin directly interacts with Na, K-ATPase. 125,126 Fodrin and ankyrin also localize to the lateral membrane of choroid plexus cells, however, 125 suggesting that the presence of these cytoskeletal linkers is not sufficient to specify Na,K-ATPase targeting.…”

Section: Cell-specific Variations In Traffickingmentioning

confidence: 99%

Trafficking to the Apical and Basolateral Membranes in Polarized Epithelial Cells

Stoops

Caplan

2014

Journal of the American Society of Nephrology

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Renal epithelial cells must maintain distinct protein compositions in their apical and basolateral membranes in order to perform their transport functions. The creation of these polarized protein distributions depends on sorting signals that designate the trafficking route and site of ultimate functional residence for each protein. Segregation of newly synthesized apical and basolateral proteins into distinct carrier vesicles can occur at the trans-Golgi network, recycling endosomes, or a growing assortment of stations along the cellular trafficking pathway. The nature of the specific sorting signal and the mechanism through which it is interpreted can influence the route a protein takes through the cell. Cell type-specific variations in the targeting motifs of a protein, as are evident for Na,K-ATPase, demonstrate a remarkable capacity to adapt sorting pathways to different developmental states or physiologic requirements. This review summarizes our current understanding of apical and basolateral trafficking routes in polarized epithelial cells.

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Section: Cell-specific Variations In Traffickingmentioning

confidence: 99%

Trafficking to the Apical and Basolateral Membranes in Polarized Epithelial Cells

Stoops

Caplan

2014

Journal of the American Society of Nephrology

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“…Ankyrin and adducin associate with spectrin and are colocalized with spectrin at sites of cell-cell contact in epithelial cells (Nelson and Veshnock, 1987a;Nelson and Hammerton, 1989;Kaiser et al, 1989). Na÷,K+-ATPase interacts with ankyrin in in vitro assays, and it is colocalized with spectrin and ankyrin in epithelial cells (Nelson and Veshnock, 1987b;Koob et al, 1988;Morrow et al, 1989). All three antibodies stain normal epithelial cells at sites of cell-cell contact.…”

Section: Localization Of Actin Ankyrin Adducin Na+k+-atpase and mentioning

confidence: 99%

Expression of functional domains of beta G-spectrin disrupts epithelial morphology in cultured cells.

Moorthy

Bennett

1995

The Journal of Cell Biology

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Abstract. Spectrin is a major structural protein associated with the cytoplasmic surface of plasma membranes of many types of cells. To study the functions of spectrin, we transfected Caco-2 intestinal epithelial cells with a plasmid conferring neomycin resistance and encoding either actin-binding or ankyrin-binding domains of beta~-spectrin fused with beta-galactosidase. These polypeptides, in principle, could interfere with the interaction of spectrin with actin or ankyrin, as well as block normal assembly of alpha-and betaspectrin subunits. Cells expressing the fusion proteins represented only a small fraction of neomycin-resistant cells, but they could be detected based on expression of beta-galactosidase. Cells expressing spectrin domains exhibited a progressive decrease in amounts of endogenous betac-spectrin, although alpha-spectrin was still present. Betac-spectrin-deficient cells lost epithelial cell morphology, became multinucleated, and eventually disappeared after 10-14 d in culture. Spectrin-associated membrane proteins, ankyrin and adducin, as well as the Na÷,K÷-ATPase, which binds to ankyrin, exhibited altered distributions in cells transfected with betac-spectrin domains. E-cadherin and F-actin, in contrast to ankyrin, adducin, and the Na÷,K÷-ATPase, were expressed, and they exhibited unaltered distribution in betao-spectrin-deficient cells. Cells transfected with the same plasmid encoding betagalactosidase alone survived in culture as the major population of neomycin-resistant cells, and they exhibited no change in morphology or in the distribution of spectrin-associated membrane proteins. These results establish that betac-spectrin is essential for the normal morphology of epithelial cells, as well as for their maintenance in monolayer culture. S PV.CTRIN is an elongated actin-binding protein that is the principal component of a system of structural proteins associated with the cytoplasmic surface of plasma membranes of most metazoan cells (reviewed by Bennett and Gilligan, 1993). Spectrin is comprised of two subunits, termed alpha and beta, that are aligned side-to-side to form heterodimers, and the dimers are linked head-to-head to form tetramers. Beta subunits contain most of the recognition sites of spectrin for other proteins including ankyrin, protein 4.1 actin, as well as the site for ankyrin-independent association of spectrin with membranes. Beta~-spectrin is the most common type of beta subunit, and it is expressed in most vertebrate tissues (Hu et al., 1992). The structure and function of spectrin has been best characterized in mammalian erythrocytes from both in vivo and in vitro studies (Palek and Lambert, 1990;Delaunay and Dhermy, 1993;Gallagher and Forget, 1993;Bennett and Gilligan, 1993). Erythrocyte spectrin forms a membrane-associated polygonal network by the associations of spectrin with actin illaments and with integral membrane proteins through linkages with ankyrin and protein 4.1. Defects and deficiencies in components of the spectrin-actin network result in abnormally fr...

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“…According to a model developed primarily by Nelson and colleagues, uvomorulin and at least some basolateral membrane proteins interact with fodrin via association with ankyrin (Nelson andVeshnock, 1986, 1987a, b;Salas et al, 1988;Morrow et al, 1989;Nelson and Hammerton, 1989;Nelson et al, 1990). Homotypic cell-cell interactions mediated by uvomorulin apparently cause the reorganization and assembly of the submembranous cytoskeleton, constraining interacting proteins to the regions of cell-cell contacts.…”

Section: Polarity Of Transformed Mdck Cellsmentioning

confidence: 99%

Multilayering and loss of apical polarity in MDCK cells transformed with viral K-ras.

Schoenenberger

Żuk

Kendall

et al. 1991

The Journal of Cell Biology

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Abstract. The effects of viral Kirsten ras oncogene expression on the polarized phenotype of MDCK cells were investigated. Stable transformed MDCK cell lines expressing the v-K-ras oncogene were generated via infection with a helper-independent retroviral vector construct. When grown on plastic substrata, transformed cells formed continuous monolayers with epithelial-like morphology. However, on permeable filter supports where normal cells form highly polarized monolayers, transformed MDCK cells detached from the substratum and developed multilayers. Morphological analysis of the multilayers revealed that oncogene expression perturbed the polarized organization of MDCK cells such that the transformed cells lacked an apical-basal axis around which the cytoplasm is normally organized. Evidence for selective disruption of apical membrane polarity was provided by immunolocalization of membrane proteins; a normally apical l l4-kD protein was randomly distributed on the cell surface in the transformed cell line, whereas normally basolateral proteins remained exclusively localized to areas of cell contact and did not appear on the free cell surface. The discrete distribution of the tight junction-associated ZO-1 protein as well as transepithelial resistance and flux measurements suggested that tight junctions were also assembled.These findings indicate that v-K-ras transformation alters cell-substratum and cell-cell interactions in MDCK cells. Furthermore, v-K-ras expression perturbs apical polarization but does not interfere with the development of a basolateral domain, suggesting that apical and basolateral polarity in epithelial ceils may be regulated independently.

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Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells.

Cited by 263 publications

References 53 publications

Trafficking to the Apical and Basolateral Membranes in Polarized Epithelial Cells

Trafficking to the Apical and Basolateral Membranes in Polarized Epithelial Cells

Expression of functional domains of beta G-spectrin disrupts epithelial morphology in cultured cells.

Multilayering and loss of apical polarity in MDCK cells transformed with viral K-ras.

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