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Vol. 10, Issue 12, 4327-4339, December 1999
Department of Cell and Molecular Biology, Northwestern University
Medical School, Chicago, Illinois 60611
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 (Kd = ~70 nM) than small
espin and was ~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 Kd of ~1 µM,
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 ~4-5 × 106 copies per ectoplasmic specialization, or ~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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