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Journal of Cell Science 115, 499-505 (2002)
© 2002 The Company of Biologists Limited

Research Article

Gelsolin — evidence for a role in turnover of junction-related actin filaments in Sertoli cells

Julian A. Guttman1,*, Paul Janmey2 and A. Wayne Vogl1

1 Department of Anatomy, 2177 Wesbrook Mall, Faculty of Medicine, The University of British Columbia, Vancouver, BC V6T 1Z3, Canada
2 Department of Physiology, Institute of Medicine and Engineering, University of Pennsylvania, 3340 Smith Walk, 1010 Vagelos Labs, Philadelphia, PA 19104, USA

* Author for correspondence (e-mail: guttman{at}interchange.ubc.ca)

Accepted 26 October 2001

The gelsolin-phosphoinositide pathway may be part of the normal mechanism by which Sertoli cells regulate sperm release and turnover of the blood-testis barrier. The intercellular adhesion complexes (ectoplasmic specializations) involved with these two processes are tripartite structures consisting of the plasma membrane, a layer of actin filaments and a cistern of endoplasmic reticulum. Gelsolin is concentrated in these adhesion complexes. In addition, phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphoinositide-specific phospholipase C are found in the structures. Treatment of isolated spermatid/junction complexes with exogenous phosphoinositide-specific phospholipase C, or with a synthetic peptide consisting of the PtdIns(4,5)P2 binding region of gelsolin, results in the release of gelsolin and loss of actin from the adhesion complexes. We present a model for the disassembly of the actin layer of the adhesion complex that involves the hydrolysis of PtdIns(4,5)P2 resulting in the release of gelsolin within the plaque. Further, we speculate that the hydrolysis of PtdIns(4,5)P2 may result in a local Ca2+ surge via the action of inositol triphosphate on junctional endoplasmic reticulum. This Ca2+ surge would facilitate the actin severing function of gelsolin within the adhesion complex.

Key words: Gelsolin, Adhesion junctions, Ectoplasmic specializations




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