ArticleProceedings of the National Academy of Sciences of the United States of America2012
Focal adhesion kinase-Tyr407 and -Tyr397 exhibit antagonistic effects on blood-testis barrier dynamics in the rat.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed, 126 citations in OpenAlex.
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- Oral administration of antimicrobial peptide MPX can effectively regulate LPS-mediated testicular oxidative stress and blood‒testis barrier damage.Scientific reports · 2025Article
- Testicular immunity.Molecular aspects of medicine · 2024Review
- PTBP1 mediates Sertoli cell actin cytoskeleton organization by regulating alternative splicing of actin regulators.Nucleic acids research · 2024Article
- PTBP1 mediates Sertoli cell actin cytoskeleton organization by regulating alternative splicing of actin regulators.bioRxiv : the preprint server for biology · 2024Article
- Blood-testis barrier: a review on regulators in maintaining cell junction integrity between Sertoli cells.Cell and tissue research · 2024Review
- Passing of Nanocarriers across the Histohematic Barriers: Current Approaches for Tumor Theranostics.Nanomaterials (Basel, Switzerland) · 2023Review
- What do we know about blood-testis barrier? current understanding of its structure and physiology.Frontiers in cell and developmental biology · 2023Review
- Sertoli cell survival and barrier function are regulated by miR-181c/d-Pafah1b1 axis during mammalian spermatogenesis.Cellular and molecular life sciences : CMLS · 2022Article
- Review
- Drug transport across the blood-testis barrier.American journal of translational research · 2022Review
- A FAKtual Retelling of Blood-Testis Barrier and Cytoskeletal Regulation.Endocrinology · 2021Article
- Disruption of anchoring junctions in the testes of experimental varicocele rats.Experimental and therapeutic medicine · 2021Article
- Microtubule-associated proteins (MAPs) in microtubule cytoskeletal dynamics and spermatogenesis.Histology and histopathology · 2021Review
- The Seminiferous Epithelial Cycle of Spermatogenesis: Role of Non-receptor Tyrosine Kinases.Advances in experimental medicine and biology · 2021Article
- Signaling Proteins That Regulate Spermatogenesis Are the Emerging Target of Toxicant-Induced Male Reproductive Dysfunction.Frontiers in endocrinology · 2021Review
- Tight junctions and their regulation by non-coding RNAs.International journal of biological sciences · 2021Review
- Integrative bioinformatics approaches for identifying potential biomarkers and pathways involved in non-obstructive azoospermia.Translational andrology and urology · 2021Article
- The Non-hormonal Male Contraceptive Adjudin Exerts its Effects via MAPs and Signaling Proteins mTORC1/rpS6 and FAK-Y407.Endocrinology · 2021Article
15 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Focal adhesion kinase (FAK), a nonreceptor protein tyrosine kinase, displays phosphorylation-dependent localization in the seminiferous epithelium of adult rat testes. FAK is an integrated component of the blood-testis barrier (BTB) involved in regulating Sertoli cell adhesion via its effects on the occludin-zonula occludens-1 complex. Herein, we report that p-FAK-Tyr(407) and p-FAK-Tyr(397) display restricted spatiotemporal and almost mutually exclusive localization in the epithelium, affecting BTB dynamics antagonistically, with the former promoting and the latter disrupting the Sertoli cell tight junction-permeability barrier function. Using primary cultured Sertoli cells as an in vitro model that mimics the BTB in vivo both functionally and ultrastructurally, effects of FAK phosphorylation on BTB function were studied by expressing nonphosphorylatable and phosphomimetic mutants, with tyrosine replaced by phenylalanine (F) and glutamate (E), respectively. Compared with WT FAK, Y407E and Y397F mutations each promoted barrier function, and the promoting effect of the Y407E mutant was abolished in the Y397E-Y407E double mutant, demonstrating antagonism between Tyr(407) and Tyr(397). Furthermore, Y407E mutation induced the recruitment of actin-related protein 3 to the Sertoli cell-cell interface, where it became more tightly associated with neuronal Wiskott-Aldrich syndrome protein, promoting actin-related protein 2/3 complex activity. Conversely, Y407F mutation reduced the rate of actin polymerization at the Sertoli cell BTB. In summary, FAK-Tyr(407) phosphorylation promotes BTB integrity by strengthening the actin filament-based cytoskeleton. FAK serves as a bifunctional molecular "switch" to direct the cyclical disassembly and reassembly of the BTB during the epithelial cycle of spermatogenesis, depending on its phosphorylation status, to facilitate the transit of preleptotene spermatocytes across the BTB.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.