Actin cross-linking protein palladin and spermatogenesis.

Spermatogenesis Pub Date : 2013-01-01 DOI:10.4161/spmg.23473
Xiaojing Qian, Dolores D Mruk, Yan Ho Cheng, C Yan Cheng
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引用次数: 13

Abstract

In the seminiferous epithelium of the mammalian testis, the most distinctive ultrastructure is the extensive bundles of actin filaments that lie near the Sertoli-spermatid interface and the Sertoli-Sertoli cell interface known as the apical ectoplasmic specialization (apical ES) and the basal ES, respectively. These actin filament bundles not only confer strong adhesion at these sites, they are uniquely found in the testis. Recent studies have shown that ES also confers spermatid and Sertoli cell polarity in the seminiferous epithelium during the epithelial cycle. While these junctions were first described in the 1970s, there are few functional studies in the literature to examine the regulation of these actin filament bundles. It is conceivable that these actin filament bundles at the ES undergo extensive re-organization to accommodate changes in location of developing spermatids during spermiogenesis as spermatids are transported across the seminiferous epithelium. Additionally, these actin filaments are rapidly reorganized during BTB restructuring to accommodate the transit of preleptotene spermatocytes across the barrier at stage VIII of the epithelial cycle. Thus, actin binding and regulatory proteins are likely involved in these events to confer changes in F-actin organization at these sites. Interestingly, there are no reports in the field to study these regulatory proteins until recently. Herein, we summarize some of the latest findings in the field regarding a novel actin cross-linker and actin-bundling protein called palladin. We also discuss in this opinion article the likely role of palladin in regulating actin filament bundles at the ES during spermatogenesis, highlighting the significant of palladin and how this protein is plausibly working in concert with other actin-binding/regulatory proteins and components of polarity proteins to regulate the cyclic events of actin organization and re-organization during the epithelial cycle of spermatogenesis. We also propose a hypothetic model by which palladin regulates ES restructuring during the epithelial cycle of spermatogenesis.

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肌动蛋白交联蛋白与精子发生。
在哺乳动物睾丸的精系上皮中,最独特的超微结构是位于支持细胞-精子界面和支持细胞-支持细胞界面附近的广泛的肌动蛋白丝束,分别被称为顶端外质特化(apical ES)和基础ES。这些肌动蛋白丝束不仅在这些部位具有很强的粘连性,而且在睾丸中才有。最近的研究表明,在上皮周期中,ES还赋予精细胞和支持细胞极性。虽然这些连接在20世纪70年代首次被描述,但文献中很少有功能研究来检查这些肌动蛋白丝束的调节。可以想象,这些肌动蛋白丝束在精子发生过程中经过广泛的重组,以适应精子在输精管上皮运输过程中发育中的精子位置的变化。此外,这些肌动蛋白丝在BTB重组过程中迅速重组,以适应在上皮周期的第VIII阶段preleptene精母细胞穿过屏障的运输。因此,肌动蛋白结合和调节蛋白可能参与了这些事件,赋予这些位点f -肌动蛋白组织的变化。有趣的是,直到最近才有研究这些调节蛋白的报道。在此,我们总结了一些最新的发现,在该领域有关一种新的肌动蛋白交联剂和肌动蛋白捆绑蛋白称为帕拉丁。在这篇观点文章中,我们还讨论了钯蛋白在精子发生过程中调节肌动蛋白丝束中的可能作用,强调了钯蛋白的重要性,以及该蛋白如何与其他肌动蛋白结合/调节蛋白和极性蛋白成分协同工作,以调节精子发生上皮周期中肌动蛋白组织和重组的循环事件。我们还提出了一个假设模型,通过该模型,palladin在精子发生的上皮周期中调节ES重组。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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Computational characterization and integrative analysis of proteins involved in spermatogenesis Genetics of mammalian meiosis Roles of membrane and nuclear estrogen receptors in spermatogenesis Androgen regulation of spermatogenesis Cytoskeletons (F-actin) and spermatogenesis
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