2006
DOI: 10.1677/joe.1.06867
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A complex containing α6β1-integrin and phosphorylated focal adhesion kinase between Sertoli cells and elongated spermatids during spermatid release from the seminiferous epithelium

Abstract: Spermiation is the final step of spermatogenesis and culminates in the disengagement (release) of elongated spermatids from Sertoli cells into the seminiferous tubule lumen. Spermiation failure, wherein spermatids are retained by Sertoli cells instead of releasing, occurs after hormone suppression. The mechanisms involved in spermatid disengagement and retention are not well understood. We previously showed that b 1 -integrin is associated with spermatids until the point of disengagement, but the ectoplasmic s… Show more

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Cited by 87 publications
(85 citation statements)
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“…1D). These findings are also consistent with earlier reports that p-FAK-Tyr 397 was crucial to maintain spermatid adhesion at stage VII-early VIII of the epithelial cycle (2,29) when its expression at the apical ES was high at these stages but it was rapidly downregulated at late stage VIII at spermiation, illustrating its overexpression might impede spermatid adhesion and transport. Indeed, overexpression of the FAK Y397E phosphomimetic mutant that mimicked p-FAK-Tyr 397 induced defects in spermiation in which elongated spermatids were entrapped in the epithelium as shown in Fig.…”
Section: Overexpression Of P-fak-tyr 397 Using a Phosphomimetic Mutansupporting
confidence: 93%
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“…1D). These findings are also consistent with earlier reports that p-FAK-Tyr 397 was crucial to maintain spermatid adhesion at stage VII-early VIII of the epithelial cycle (2,29) when its expression at the apical ES was high at these stages but it was rapidly downregulated at late stage VIII at spermiation, illustrating its overexpression might impede spermatid adhesion and transport. Indeed, overexpression of the FAK Y397E phosphomimetic mutant that mimicked p-FAK-Tyr 397 induced defects in spermiation in which elongated spermatids were entrapped in the epithelium as shown in Fig.…”
Section: Overexpression Of P-fak-tyr 397 Using a Phosphomimetic Mutansupporting
confidence: 93%
“…Herein, we demonstrate that p-FAK-Tyr 397 is one of the major players in these events. Unlike other epithelia in which FAK is restricted to the cell-extracellular matrix interface known as the focal adhesion complex (FAC) or focal contact that mediates integrin-based signaling to regulate cell movement (3, 7), p-FAK-Tyr 397 was first demonstrated to be a component of the apical ES (2,29) that displayed stage-specific and spatiotemporal expression in the rat testis (29 . FAK Y397E mutant-induced defects in spermiation in the rat testis are mediated by retention of nectin-3 at the apical ES.…”
Section: Discussionmentioning
confidence: 99%
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“…However, the BTB undergoes cyclical restructuring to allow the transit of preleptotene spermatocytes from the basal to the adluminal compartment in the rat (1,2), implying that these filament bundles undergo extensive reorganization. Previous studies have shown that focal adhesion kinase (FAK) is predominantly localized in the seminiferous epithelium near the basement membrane at the site of the BTB (3), whereas its phosphorylated form, p-FAKTyr 397 , is almost exclusively restricted to the apical ES (3,4) [a filamentous (F)-actin-rich testis-specific AJ, analogous to the basal ES structurally but limited to the Sertoli cell-spermatid interface, which also undergoes cyclical remodeling to facilitate spermatid movement across the epithelium during spermiogenesis (2, 5)].…”
mentioning
confidence: 99%