Abstract
The ectoplasmic specialization is thought to anchor and position spermatids within the seminiferous epithelium throughout much of spermiogenesis. It may also contribute to the “blood—testis” barrier between Sertoli cells (1,2). These activities are believed to depend critically on the ectoplasmic specialization junctional plaque, which is characterized by a layer of parallel actin bundles sandwiched between the Sertoli-cell plasma membrane and a cistern of endoplasmic reticulum (1,2). The parallel actin bundles are believed to act both as a scaffold that supports and stabilizes an adhesive domain within the overlying Sertoli-cell plasma membrane and indirectly, via the cistern of endoplasmic reticulum, as a link to an underlying network of microtubules to allow for changes in the position of the ectoplasmic specialization—spermatid complex (1,2).
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Vogl AW, Pfeiffer DC, Redenbach DM. Ectoplasmic (“junctional”) specializations in mammalian Sertoli cells: influence on spermatogenic cells. Ann NY Acad Sci 1991; 637: 175 – 202.
Russell LD, Peterson RN. Sertoli cell junctions: morphological and functional correlates. Int Rev Cytol 1985; 94: 177 – 211.
Bartles JR, Wierda A, Zheng L. Identification and characterization of espin, an actin-binding protein localized to the F-actin-rich junctional plaques of Sertoli cell ectoplasmic specializations. J Cell Sci 1989; 109: 1229 – 39.
Bartles JR, Zheng L, Li A, Wierda A, Chen B. Small espin: a third actin-bundling protein and potential forked protein ortholog in brush border microvilli. J Cell Biol 1998;143:107–19.
Hoover KK, Chien AJ, Corces VG. Effect of transposable elements on the expression of the forked gene of Drosophila melanogaster. Genetics 1993;135:507–26.
Heintzelman MB, Mooseker M. Assembly of the intestinal brush border cytoskeleton. Curr Top Dev Biol 1992;26:93–122.
Glenney JR Jr, Kaulfus P, Matsudaira P, Weber K. F-actin binding and bundling properties of fimbrin, a major cytoskeletal protein of microvillus core filaments. J Biol Chem 1981;256:9283–88.
Burgess DR, Broschat KO, Hayden JM. Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins. J Cell Biol 1987;104:29–40.
Pollard TD . Actin and actin-binding proteins. In: Kreis T, Vale R, eds. Guidebook to the cytoskeletal and motor proteins. Oxford: Oxford University Press, 1993:3–11.
Tilney LG, Tilney MS, Guild GM. F-Actin bundles in Drosophila bristles. I. Two filament cross-links are involved in bundling. J Cell Biol 1995;130:629–38.
Tang JX, Janmey PA. The polyeleetrolyte nature of F-actin and the mechanism of actin bundle formation. J Biol Chem 1996;271:8556–63.
Puius Y, Mahoney NM, Almo SC. The modular structure of actin-regulatory proteins. Curr Opin Cell Biol 1998;10:23–34.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2000 Springer-Verlag New York, Inc.
About this paper
Cite this paper
Bartles, J.R., Zheng, L., Wang, M., Chen, B. (2000). The Actin-Bundling Protein Espin and Its Role in the Ectoplasmic Specialization. In: Goldberg, E. (eds) The Testis. Serono Symposia USA. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-2106-7_14
Download citation
DOI: https://doi.org/10.1007/978-1-4612-2106-7_14
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4612-7416-2
Online ISBN: 978-1-4612-2106-7
eBook Packages: Springer Book Archive