Dataset Information

Fascin - An actin binding and bundling protein in the testis and its role in ectoplasmic specialization dynamics.

ABSTRACT: In the mammalian testis such as in rats, a unique actin-rich cell-cell adherens junction (AJ) known as ectoplasmic specialization (ES) is found in the seminiferous epithelium. ES is conspicuously found between Sertoli cells near the basement membrane known as the basal ES, which together with tight junction (TJ), gap junction, and desmosome constitute the blood-testis barrier (BTB). The BTB, in turn, anatomically divides the seminiferous epithelium into the basal and the adluminal (apical) compartment. On the other hand, ES is also found at the Sertoli-spermatid interface known as apical ES which is the only anchoring device for developing step 8-19 spermatids during spermiogenesis. One of the most typical features of the ES is the array of actin microfilament bundles that lie perpendicular to the Sertoli cell plasma membrane and are sandwiched in-between the cisternae of endoplasmic reticulum and the Sertoli cell plasma membrane. While these actin filament bundles confer the adhesive strength of Sertoli cells at the BTB and also spermatids in the adluminal compartment, they must be rapidly re-organized from their bundled to unbundled/branched configuration and vice versa to provide plasticity to the ES so that preleptotene spermatocytes and spermatids can be transported across the immunological barrier and the adluminal compartment, respectively, during the epithelial cycle of spermatogenesis. Fascin is a family of actin microfilament cross-linking and bundling proteins that is known to confer bundling of parallel actin microfilaments in mammalian cells. A recent report has illustrated the significance of a fascin protein called fascin 1 in actin microfilaments at the ES, pertinent to its role in spermatogenesis (Gungor-Ordueri et al. Am J Physiol Endocrinol Metab 307, E738-753, 2004 (DOI:10.1152/ajpendo.00113.2014). In this Commentary, we critically evaluate these findings in light of the role of fascin in other mammalian cells, providing some insightful information for future investigations.

SUBMITTER: Gungor-Ordueri NE

PROVIDER: S-EPMC4581068 | biostudies-other | 2015 Jan-Apr

REPOSITORIES: biostudies-other

ACCESS DATA

Similar Datasets

Project description:Ectoplasmic specialization (ES) is an actin-rich adherens junction in the seminiferous epithelium of adult mammalian testes. ES is restricted to the Sertoli-spermatid (apical ES) interface, as well as the Sertoli cell-cell (basal ES) interface at the blood-testis barrier (BTB). ES is typified by the presence of an array of bundles of actin microfilaments near the Sertoli cell plasma membrane. These actin microfilament bundles require rapid debundling to convert them from a bundled to branched/unbundled configuration and vice versa to confer plasticity to support the transport of 1) spermatids in the adluminal compartment and 2) preleptotene spermatocytes at the BTB while maintaining cell adhesion. Plastin 3 is one of the plastin family members abundantly found in yeast, plant and animal cells that confers actin microfilaments their bundled configuration. Herein, plastin 3 was shown to be a component of the apical and basal ES in the rat testis, displaying spatiotemporal expression during the epithelial cycle. A knockdown (KD) of plastin 3 in Sertoli cells by RNA interference using an in vitro model to study BTB function showed that a transient loss of plastin 3 perturbed the Sertoli cell tight junction-permeability barrier, mediated by changes in the localization of basal ES proteins N-cadherin and β-catenin. More importantly, these changes were the result of an alteration of the actin microfilaments, converting from their bundled to branched configuration when examined microscopically, and validated by biochemical assays that quantified actin-bundling and polymerization activity. Moreover, these changes were confirmed by studies in vivo by plastin 3 KD in the testis in which mis-localization of N-cadherin and β-catenin was also detected at the BTB, concomitant with defects in the transport of spermatids and phagosomes and a disruption of cell adhesion most notably in elongated spermatids due to a loss of actin-bundling capability at the apical ES, which in turn affected localization of adhesion protein complexes at the site. In summary, plastin 3 is a regulator of actin microfilament bundles at the ES in which it dictates the configuration of the filamentous actin network by assuming either a bundled or unbundled/branched configuration via changes in its spatiotemporal expression during the epithelial cycle.

Dataset Information

Fascin - An actin binding and bundling protein in the testis and its role in ectoplasmic specialization dynamics.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets