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{Chen1999EspinCA,
  title={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.},
  author={Benjamin Jieming Chen and Anli Li and Demin Wang and M Wang and Lili Zheng and James R. Bartles},
  journal={Molecular biology of the cell},
  year={1999},
  volume={10 12},
  pages={
          4327-39
        }
}
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… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 37 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 50 references

Histological and Histopathological Evaluation of the Testis

L. D. Russell, R. A. Ettlin, A.P.S. Hikim, E. D. Clegg
1990
View 5 Excerpts
Highly Influenced

Sertoli cell junctions: morphological and functional correlates.

International review of cytology • 1985
View 7 Excerpts
Highly Influenced

How actin filaments pack into bundles.

Cold Spring Harbor symposia on quantitative biology • 1982
View 4 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…