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Abstract

Volume 18, Issue 5 (September 2016) 18, 716–722; DOI:10.4103/1008-682X.166583

Plastins regulate ectoplasmic specialization via its actin bundling activity on microfilaments in the rat testis

Nan Li, Chris KC Wong, C Yan Cheng

1 The Mary M. Wohlford Laboratory for Male Contraceptive Research, Center for Biomedical Research, Population Council, 1230 York Avenue, New York 10065, USA
2 Department of Biology, Hong Kong Baptist University, Hong Kong, China


Correspondence: Dr. CY Cheng (Y‑Cheng@popcbr.rockefeller.edu)

20-Nov-2015

Abstract

Abstract

Plastins are a family of actin binding proteins (ABPs) known to cross-link actin microfilaments in mammalian cells, creating actin microfilament bundles necessary to confer cell polarity and cell shape. Plastins also support cell movement in response to changes in environment, involved in cell/tissue growth and development. They also confer plasticity to cells and tissues in response to infection or other pathological conditions (e.g., inflammation). In the testis, the cell-cell anchoring junction unique to the testis that is found at the Sertoli cell-cell interface at the blood-testis barrier (BTB) and at the Sertoli-spermatid (e.g., 8-19 spermatids in the rat testis) is the basal and the apical ectoplasmic specialization (ES), respectively. The ES is an F-actin-rich anchoring junction constituted most notably by actin microfilament bundles. A recent report using RNAi that specifically knocks down plastin 3 has yielded some insightful information regarding the mechanism by which plastin 3 regulates the status of actin microfilament bundles at the ES via its intrinsic actin filament bundling activity. Herein, we provide a brief review on the role of plastins in the testis in light of this report, which together with recent findings in the field, we propose a likely model by which plastins regulate ES function during the epithelial cycle of spermatogenesis via their intrinsic activity on actin microfilament organization in the rat testis.

Keywords: actin binding proteins; actin bundling proteins; cytoskeleton; F-actin; fimbrins; plastins; seminiferous epithelial cycle; spermatogenesis; testis


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