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Article: Actin-binding protein drebrin E is involved in junction dynamics during spermatogenesis

TitleActin-binding protein drebrin E is involved in junction dynamics during spermatogenesis
Authors
KeywordsTestis
Spermatogenesis
Blood-testis barrier
Drebrin E
Actin-binding protein
Issue Date2011
PublisherLandes Bioscience. The Journal's web site is located at http://www.landesbioscience.com/journals/spermatogenesis/
Citation
Spermatogenesis, 2011, v. 1 n. 2, p. 123-136 How to Cite?
AbstractThe actin-based cytoskeleton plays a critical role in the seminiferous epithelium during spermatogenesis by conferring cell shape, adhesion, structural support and cell polarity to both Sertoli and developing germ cells, which are essential for spermatogonial stem cell renewal, maintenance of the stem cell niche, cell cycle progression, mitosis, meiosis, spermiogenesis and spermiation. However, few functional studies are found in the literature, which explore the functional significance of actin dynamics in these events. This by and large is due to a lack of information on the proteins that regulate actin dynamics. Herein, we report drebrin E is an integrated component of the apical ectoplasmic specialization (apical ES) and the basal ES at the blood-testis barrier (BTB) in the seminiferous epithelium of the adult rat testis. Using immunohistochemistry and dual-labeled immunofluorescence analysis, drebrin E was found to display a stage-specific localization at the apical ES, as well as at the basal ES at the BTB during the seminiferous epithelial cycle of spermatogenesis. Drebrin E was first detected in stage V tubules at the basal ES with the highest expression at the BTB at stages V and VI, but it diminished considerably by stages VII and VIII and was almost non-detectable until stage IV. At the apical ES, drebrin E was also first detected at stage V, surrounding the entire head of the elongating spermatid, but by stage VI its localization had 'shifted' to localize most intensely and almost exclusively to the concave side of the spermatid head. In stage VII tubules, drebrin E co-localized with actin, as well as with two other actin regulatory proteins Eps8 (epidermal growth factor receptor pathway substrate 8, an actin capping and bundling protein) and Arp3 (actin-related protein 3, a component of the Arp2/3 complex known to regulate actin nucleation and branching). The localization of drebrin E at the apical ES was compromised following treatment of rats with adjudin, which is known to exert its destructive effects primarily at the apical ES by inducing premature loss of elongating/elongated spermatids from the epithelium, mimicking 'spermiation.' Instead of being restricted to the concave side of spermatid heads, drebrin E was found to be mis-localized in the seminiferous epithelium of adjudin-treated rats; it was also present on the convex side of elongating spermatids, but these cells were mis-oriented so that their heads no longer pointed toward the basement membrane. The expression of drebrin E by Sertoli cells was also found to be modulated by TGFbeta3 and TNFalpha. Since Arp3, but not Eps8, was found to bind drebrin E; and cytokines were also shown to affect the cellular distribution of drebrin E and enhance the interaction between drebrin E and Arp3, these findings illustrate that cytokines may regulate BTB dynamics during the epithelial cycle by recruiting drebrin E and Arp3 to the BTB microenvironment to induce changes in the configuration of actin filament bundles at the basal ES. In summary, these findings illustrate drebrin E is working in concert with Arp3 to regulate actin filament bundles at both the apical and the basal ES in the testis, conferring adhesion and cell polarity at both sites during spermatogenesis.
Persistent Identifierhttp://hdl.handle.net/10722/138078
ISSN
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorLi, MWMen_US
dc.contributor.authorXiao, Xen_US
dc.contributor.authorMruk, DDen_US
dc.contributor.authorLam, YLen_US
dc.contributor.authorLee, WWMen_US
dc.contributor.authorLui, WYen_US
dc.contributor.authorBonanomi, Men_US
dc.contributor.authorSilvestrini, Ben_US
dc.contributor.authorCheng, CYen_US
dc.date.accessioned2011-08-26T14:39:42Z-
dc.date.available2011-08-26T14:39:42Z-
dc.date.issued2011en_US
dc.identifier.citationSpermatogenesis, 2011, v. 1 n. 2, p. 123-136en_US
dc.identifier.issn2156-5554-
dc.identifier.urihttp://hdl.handle.net/10722/138078-
dc.description.abstractThe actin-based cytoskeleton plays a critical role in the seminiferous epithelium during spermatogenesis by conferring cell shape, adhesion, structural support and cell polarity to both Sertoli and developing germ cells, which are essential for spermatogonial stem cell renewal, maintenance of the stem cell niche, cell cycle progression, mitosis, meiosis, spermiogenesis and spermiation. However, few functional studies are found in the literature, which explore the functional significance of actin dynamics in these events. This by and large is due to a lack of information on the proteins that regulate actin dynamics. Herein, we report drebrin E is an integrated component of the apical ectoplasmic specialization (apical ES) and the basal ES at the blood-testis barrier (BTB) in the seminiferous epithelium of the adult rat testis. Using immunohistochemistry and dual-labeled immunofluorescence analysis, drebrin E was found to display a stage-specific localization at the apical ES, as well as at the basal ES at the BTB during the seminiferous epithelial cycle of spermatogenesis. Drebrin E was first detected in stage V tubules at the basal ES with the highest expression at the BTB at stages V and VI, but it diminished considerably by stages VII and VIII and was almost non-detectable until stage IV. At the apical ES, drebrin E was also first detected at stage V, surrounding the entire head of the elongating spermatid, but by stage VI its localization had 'shifted' to localize most intensely and almost exclusively to the concave side of the spermatid head. In stage VII tubules, drebrin E co-localized with actin, as well as with two other actin regulatory proteins Eps8 (epidermal growth factor receptor pathway substrate 8, an actin capping and bundling protein) and Arp3 (actin-related protein 3, a component of the Arp2/3 complex known to regulate actin nucleation and branching). The localization of drebrin E at the apical ES was compromised following treatment of rats with adjudin, which is known to exert its destructive effects primarily at the apical ES by inducing premature loss of elongating/elongated spermatids from the epithelium, mimicking 'spermiation.' Instead of being restricted to the concave side of spermatid heads, drebrin E was found to be mis-localized in the seminiferous epithelium of adjudin-treated rats; it was also present on the convex side of elongating spermatids, but these cells were mis-oriented so that their heads no longer pointed toward the basement membrane. The expression of drebrin E by Sertoli cells was also found to be modulated by TGFbeta3 and TNFalpha. Since Arp3, but not Eps8, was found to bind drebrin E; and cytokines were also shown to affect the cellular distribution of drebrin E and enhance the interaction between drebrin E and Arp3, these findings illustrate that cytokines may regulate BTB dynamics during the epithelial cycle by recruiting drebrin E and Arp3 to the BTB microenvironment to induce changes in the configuration of actin filament bundles at the basal ES. In summary, these findings illustrate drebrin E is working in concert with Arp3 to regulate actin filament bundles at both the apical and the basal ES in the testis, conferring adhesion and cell polarity at both sites during spermatogenesis.-
dc.languageengen_US
dc.publisherLandes Bioscience. The Journal's web site is located at http://www.landesbioscience.com/journals/spermatogenesis/-
dc.relation.ispartofSpermatogenesisen_US
dc.subjectTestis-
dc.subjectSpermatogenesis-
dc.subjectBlood-testis barrier-
dc.subjectDrebrin E-
dc.subjectActin-binding protein-
dc.titleActin-binding protein drebrin E is involved in junction dynamics during spermatogenesisen_US
dc.typeArticleen_US
dc.identifier.emailLee, WWM: hrszlwm@hku.hken_US
dc.identifier.emailLui, WY: wylui@hku.hken_US
dc.identifier.authorityLee, WWM=rp00728en_US
dc.identifier.authorityLui, WY=rp00756en_US
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.4161/spmg.1.2.16393-
dc.identifier.pmid22319661-
dc.identifier.pmcidPMC3271655-
dc.identifier.hkuros191899en_US
dc.identifier.volume1en_US
dc.identifier.issue2-
dc.identifier.spage123en_US
dc.identifier.epage136en_US
dc.publisher.placeUnited States-

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