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First published online 24 November 2009
doi: 10.1242/jcs.058263

Journal of Cell Science 122, 4547-4557 (2009)
Published by The Company of Biologists 2009
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Research Article

CaMKII{alpha} interacts with multi-PDZ domain protein MUPP1 in spermatozoa and prevents spontaneous acrosomal exocytosis

Frauke Ackermann1,2,*, Nele Zitranski3,*, Heike Borth2,3, Thomas Buech3, Thomas Gudermann3 and Ingrid Boekhoff2,3,{ddagger}

1 Karolinska Institute, Department of Neuroscience, Stockholm, Sweden
2 Institute of Pharmacology and Toxicology, Philipps-University, Marburg, Germany
3 Walther Straub-Institute of Pharmacology and Toxicology, Ludwig-Maximilians-University, Munich, Germany

{ddagger} Author for correspondence (ingrid.boekhoff{at}lrz.uni-muenchen.de)

Accepted 7 October 2009

The success of acrosomal exocytosis, a complex process with a variety of inter-related steps, relies on the coordinated interaction of participating signaling molecules. Since the acrosome reaction resembles Ca2+-regulated exocytosis in neurons, we investigated whether cognate neuronal binding partners of the multi-PDZ domain protein MUPP1, which recruits molecules that control the initial tethering and/or docking between the acrosomal vesicle and the plasma membrane, are also expressed in spermatozoa, and whether they contribute to the regulation of acrosomal secretion. We observed that CaMKII{alpha} colocalizes with MUPP1 in the acrosomal region of epididymal spermatozoa where the kinase selectively binds to a region encompassing PDZ domains 10-11 of MUPP1. Furthermore, we found that pre-treating mouse spermatozoa with a CaMKII inhibitor that directly blocks the catalytic region of the kinase, as well as a competitive displacement of CaMKII{alpha} from PDZ domains 10-11, led to a significant increase in spontaneous acrosomal exocytosis. Since Ca2+-calmodulin releases CaMKII{alpha} from the PDZ scaffolding protein, MUPP1 represents a central signaling platform to dynamically regulate the assembly and disassembly of binding partners pertinent to acrosomal secretion, thereby precisely adjusting an increase in Ca2+ to synchronized fusion pore formation.

Key words: Acrosome reaction, CaMKII, MUPP1, Calcium-regulated exocytosis, Spermatozoa, PDZ domain, Lipid rafts, Scaffolding protein


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JCS 2009 122: 2402. [Full Text]  





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