ArticleThe international journal of biochemistry & cell biology2011
c-Yes regulates cell adhesion at the blood-testis barrier and the apical ectoplasmic specialization in the seminiferous epithelium of rat testes.
Article in The international journal of biochemistry & cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 73 citations in OpenAlex.
- Inflammation-Driven Remodeling of the Blood-Testis Barrier: Roles of Junctional Complexes, Actin Dynamics, and Kinase Signaling.Biomedicines · 2026Review
- Occludin: a gatekeeper of brain Infection by HIV-1.Fluids and barriers of the CNS · 2023Review
- What do we know about blood-testis barrier? current understanding of its structure and physiology.Frontiers in cell and developmental biology · 2023Review
- Matrine Regulates Proliferation, Apoptosis, Cell Cycle, Migration, and Invasion of Non-Small Cell Lung Cancer Cells Through the circFUT8/miR-944/YES1 Axis.Cancer management and research · 2021Article
- Effect of miR-140-5p on the regulation of proliferation and apoptosis in NSCLC and its underlying mechanism.Experimental and therapeutic medicine · 2019Article
- Emerging role for SRC family kinases in junction dynamics during spermatogenesis.Reproduction (Cambridge, England) · 2019Review
- Src family kinases (SFKs) and cell polarity in the testis.Seminars in cell & developmental biology · 2018Review
- Signaling pathways regulating blood-tissue barriers - Lesson from the testis.Biochimica et biophysica acta. Biomembranes · 2018Review
- Article
- Regulation of the blood-testis barrier by a local axis in the testis: role of laminin α2 in the basement membrane.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017Article
- Formin 1 Regulates Microtubule and F-Actin Organization to Support Spermatid Transport During Spermatogenesis in the Rat Testis.Endocrinology · 2016Article
- Planar Cell Polarity (PCP) Protein Vangl2 Regulates Ectoplasmic Specialization Dynamics via Its Effects on Actin Microfilaments in the Testes of Male Rats.Endocrinology · 2016Article
- Overexpression of plastin 3 in Sertoli cells disrupts actin microfilament bundle homeostasis and perturbs the tight junction barrier.Spermatogenesis · 2016Article
- Regulation of blood-testis barrier by actin binding proteins and protein kinases.Reproduction (Cambridge, England) · 2016Review
- Mouse Spermatogenesis Requires Classical and Nonclassical Testosterone Signaling.Biology of reproduction · 2016Article
- The Mammalian Blood-Testis Barrier: Its Biology and Regulation.Endocrine reviews · 2015Review
- Actin-bundling protein plastin 3 is a regulator of ectoplasmic specialization dynamics during spermatogenesis in the rat testis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- Formin 1 Regulates Ectoplasmic Specialization in the Rat Testis Through Its Actin Nucleation and Bundling Activity.Endocrinology · 2015Article
- Actin binding proteins in blood-testis barrier function.Current opinion in endocrinology, diabetes, and obesity · 2015Review
- Fascin 1 is an actin filament-bundling protein that regulates ectoplasmic specialization dynamics in the rat testis.American journal of physiology. Endocrinology and metabolism · 2014Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
During spermatogenesis, extensive junction restructuring takes place at the blood-testis barrier (BTB) and the Sertoli cell-spermatid interface known as the apical ectoplasmic specialization (apical ES, a testis-specific adherens junction) in the seminiferous epithelium. However, the mechanism(s) that regulates these critical events in the testis remains unknown. Based on the current concept in the field, changes in the phosphorylation status of integral membrane proteins at these sites can induce alterations in protein endocytosis and recycling, causing junction restructuring. Herein, c-Yes, a non-receptor protein tyrosine kinase, was found to express abundantly at the BTB and apical ES stage-specifically, coinciding with junction restructuring events at these sites during the seminiferous epithelial cycle of spermatogenesis. c-Yes also structurally associated with adhesion proteins at the BTB (e.g., occludin and N-cadherin) and the apical ES (e.g., β1-integrin, laminins β3 and γ3), possibly to regulate phosphorylation status of proteins at these sites. SU6656, a selective c-Yes inhibitor, was shown to perturb the Sertoli cell tight junction-permeability barrier in vitro, which is mediated by changes in the distribution of occludin and N-cadherin at the cell-cell interface, moving from cell surface to cytosol, thereby destabilizing the tight junction-barrier. However, this disruptive effect of SU6656 on the barrier was blocked by testosterone. Furthermore, c-Yes is crucial to maintain the actin filament network in Sertoli cells since a blockade of c-Yes by SU6656 induced actin filament disorganization. In summary, c-Yes regulates BTB and apical ES integrity by maintaining proper distribution of integral membrane proteins and actin filament organization at these sites.
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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.