Localization of nonerythroid spectrin and actin in mouse oocytes and preimplantation embryos

Reima, Ilkka; Lehtonen, Eero

doi:10.1111/j.1432-0436.1985.tb00515.x

Cited by 48 publications

(30 citation statements)

References 36 publications

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“…Little biochemical work has yet been undertaken on the actin-associated proteins. The suggestion that alpha-spectrin was totally lacking in the oocyte and appeared fi rst at the 2-cell stage (Sobel & Alliegro 1985) has not been substantiated (Reima & Lehtonen 1985;Damjanov et aI1986).…”

Section: Actin and Actin-associated Proteinsmentioning

confidence: 95%

From Egg to Epithelium

Fleming¹,

Johnson²

1988

Annu. Rev. Cell. Biol.

228

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Section: Actin and Actin-associated Proteinsmentioning

confidence: 95%

From Egg to Epithelium

Fleming¹,

Johnson²

1988

Annu. Rev. Cell. Biol.

228

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“…reported to co-localize with E-cadherin at sites of cell-cell contact in eight-cell mouse embryos (31,32). We detected 190-kDa ankyrin-G and 270-kDa ␤-2-spectrin in immunoblots of early mouse embryos using affinity-purified polyclonal antibodies (supplemental Fig.…”

Section: E-cadherin Requires Ankyrin-g and ␤-2-spectrin In Earlymentioning

confidence: 99%

Ankyrin-G Is a Molecular Partner of E-cadherin in Epithelial Cells and Early Embryos

Kizhatil

Davis

et al. 2007

Journal of Biological Chemistry

129

139

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E-cadherin is a ubiquitous component of lateral membranes in epithelial tissues and is required to form the first lateral membrane domains in development. Here, we identify ankyrin-G as a molecular partner of E-cadherin and demonstrate that ankyrin-G and ␤-2-spectrin are required for accumulation of E-cadherin at the lateral membrane in both epithelial cells and early embryos. Ankyrin-G binds to the cytoplasmic domain of E-cadherin at a conserved site distinct from that of ␤-catenin. Ankyrin-G also recruits ␤-2-spectrin to E-cadherin-␤-catenin complexes, thus providing a direct connection between E-cadherin and the spectrin/actin skeleton. In addition to restricting the membrane mobility of E-cadherin, ankyrin-G and ␤-2-spectrin also are required for exit of E-cadherin from the trans-Golgi network in a microtubule-dependent pathway. Ankyrin-G and ␤-2-spectrin co-localize with E-cadherin in preimplantation mouse embryos. Moreover, knockdown of either ankyrin-G or ␤-2-spectrin in one cell of a two-cell embryo blocks accumulation of E-cadherin at sites of cell-cell contact. E-cadherin thus requires both ankyrin-G and ␤-2-spectrin for its cellular localization in early embryos as well as cultured epithelial cells. We have recently reported that ankyrin-G and ␤-2-spectrin collaborate in biogenesis of the lateral membrane (

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“…Recent immunolocalization studies of egg spectrin in sea urchin oogenesis support the idea that spectrin is a developmentally expressed cytoplasmic protein which assembles onto cytoplasmic vesicles during egg maturation [Fishkind et al, 19881. By both metabolic labeling [Sobel and Goldstein, 19881 and immunofluorescence [Reima and Lehtonen, 1985;Sobel and Alliegro, 1985;Damjanov et al, 1986;Schatten et al, 1986;Sobel et al, 19881, in mouse and sea urchin embryos [Schatten et al, 1986;Fishkind et al, 19881 nonerythroid spectrin appears to be developmentally regulated. During murine development, nonerythroid a-spectrin is present at areas of cell-cell contact, frequently in a cortical band, but it is also present cytoplasmically in postimplant embryos [Damjanov et al, 1986;Schatten et al, 19861.…”

Section: Dynamic Expression/regulationmentioning

confidence: 99%

Functional diversity among spectrin isoforms

Coleman

Fishkind

Mooseker

et al. 1989

Cell Motil. Cytoskeleton

115

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The purpose of this review on spectrin is to examine the functional properties of this ubiquitous family of membrane skeletal proteins. Major topics include spectrin-membrane linkages, spectrin-filament linkages, the subcellular localization of spectrins in various cell types and a discussion of major functional differences between erythroid and nonerythroid spectrins. This includes a summary of studies from our own laboratories on the functional and structural comparison of avian spectrin isoforms which are comprised of a common alpha subunit and a tissue-specific beta subunit. Consequently, the observed differences among these spectrins can be assigned to differences in the properties of the beta subunits.

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Localization of nonerythroid spectrin and actin in mouse oocytes and preimplantation embryos

Cited by 48 publications

References 36 publications

From Egg to Epithelium

From Egg to Epithelium

Ankyrin-G Is a Molecular Partner of E-cadherin in Epithelial Cells and Early Embryos

Functional diversity among spectrin isoforms

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