ArticleMolecular biology of the cell1999
Espin contains an additional actin-binding site in its N terminus and is a major actin-bundling protein of the Sertoli cell-spermatid ectoplasmic specialization junctional plaque.
Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 88 citations in OpenAlex.
- Ultra-Low Temperature Cryopreservation of Sperm from a New Type of Hybrid Bream.International journal of molecular sciences · 2026Article
- Synergistic assembly, disassembly, and protection of complex forms of bundled F-actin.The Journal of cell biology · 2026Article
- Taperin bundles F-actin at stereocilia pivot points enabling optimal lifelong mechanosensitivity.The Journal of cell biology · 2025Article
- 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
- The actin cytoskeleton in hair bundle development and hearing loss.Hearing research · 2023Review
- Actin Bundles Dynamics and Architecture.Biomolecules · 2023Review
- Studies of functional properties of espin 1: Its interaction to actin filaments.Frontiers in cell and developmental biology · 2022Article
- Diverse functions of myosin VI in spermiogenesis.Histochemistry and cell biology · 2021Review
- Semi-automated single-molecule microscopy screening of fast-dissociating specific antibodies directly from hybridoma cultures.Cell reports · 2021Article
- Qualitative analysis of contribution of intracellular skeletal changes to cellular elasticity.Cellular and molecular life sciences : CMLS · 2020Review
- Identification of whirlin domains interacting with espin: A study of the mechanism of Usher syndrome type II.Molecular medicine reports · 2019Article
- mDia1/3 generate cortical F-actin meshwork in Sertoli cells that is continuous with contractile F-actin bundles and indispensable for spermatogenesis and male fertility.PLoS biology · 2018Article
- Inframe deletion of humanJournal of medical genetics · 2018Article
- Article
- Comparative effects of di(n-butyl) phthalate exposure on fetal germ cell development in the rat and in human fetal testis xenografts.Environmental health perspectives · 2015Article
- New insights into FAK function and regulation during spermatogenesis.Histology and histopathology · 2014Review
- Characterization and regulation of an additional actin-filament-binding site in large isoforms of the stereocilia actin-bundling protein espin.Journal of cell science · 2014Article
- Whirlin interacts with espin and modulates its actin-regulatory function: an insight into the mechanism of Usher syndrome type II.Human molecular genetics · 2012Article
- The effect of secretory factors of adipose-derived stem cells on human keratinocytes.International journal of molecular sciences · 2012Article
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6 authors at 1 institution in 1 country.
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Abstract
The espins are actin-binding and -bundling proteins localized to parallel actin bundles. The 837-amino-acid "espin" of Sertoli cell-spermatid junctions (ectoplasmic specializations) and the 253-amino-acid "small espin" of brush border microvilli are splice isoforms that share a C-terminal 116-amino-acid actin-bundling module but contain different N termini. To investigate the roles of espin and its extended N terminus, we examined the actin-binding and -bundling properties of espin constructs and the stoichiometry and developmental accumulation of espin within the ectoplasmic specialization. An espin construct bound to F-actin with an approximately threefold higher affinity (K(d) = approximately 70 nM) than small espin and was approximately 2.5 times more efficient at forming bundles. The increased affinity appeared to be due to an additional actin-binding site in the N terminus of espin. This additional actin-binding site bound to F-actin with a K(d) of approximately 1 microM, decorated actin stress fiber-like structures in transfected cells, and was mapped to a peptide between the two proline-rich peptides in the N terminus of espin. Espin was detected at approximately 4-5 x 10(6) copies per ectoplasmic specialization, or approximately 1 espin per 20 actin monomers and accumulated there coincident with the formation of parallel actin bundles during spermiogenesis. These results suggest that espin is a major actin-bundling protein of the Sertoli cell-spermatid ectoplasmic specialization.
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