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BOR - Papers in Press, published online ahead of print September 1, 2004.
Biol Reprod 2004, 10.1095/biolreprod.104.030866
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BIOLOGY OF REPRODUCTION 72, 14–21 (2005)
DOI: 10.1095/biolreprod.104.030866
© 2005 by the Society for the Study of Reproduction, Inc.

The Deubiquitinating Enzyme mUBPy Interacts with the Sperm-Specific Molecular Chaperone MSJ-1: The Relation with the Proteasome, Acrosome, and Centrosome in Mouse Male Germ Cells1

Giovanna Berruti2,3, and Enzo Martegani4

Dipartimento di Biologia,3 Università di Milano, 20133 Milano, Italy Dipartimento di Biotecnologie e Bioscienze,4 Università di Milano-Bicocca, 20126 Milano, Italy

The mouse USP8/mUBPy gene codifies a deubiquitinating enzyme expressed preferentially in testis and brain. While the ubiquitin-specific processing proteases (UBPs) are known to be important for the early development in invertebrate organisms, their specific functions remain still unclear in mammals. Using specific antibodies, raised against a recombinant mUBPy protein, we studied mUBPy in mouse testis. The mUBPy is expressed exclusively by the germ cell component and is maintained in epididymal spermatozoa. The enzyme is functionally active, being able to detach ubiquitin moieties from endogenous protein substrates. Protein interaction assays showed that sperm UBPy interacts with MSJ-1, the sperm-specific DnaJ protein evolutionarily conserved for spermiogenesis. Immunocytochemistry revealed that mUBPy shares with MSJ-1 the intracellular localization during spermatid cell differentiation; intriguingly, we show here that the proteasomes also locate in mUBPy/MSJ-1-positive sites, such as the cytoplasmic surface of the developing acrosome and the centrosomal region. These colocalization sites are maintained in epididymal spermatozoa. The demonstration of a protein interaction between a deubiquitinating enzyme and a molecular chaperone and the documentation on the proteasomes in both differentiating and mature mouse male germ cells suggest that members of the chaperone and ubiquitin/proteasome systems could cooperate in the fine control of protein quality to yield functional spermatozoa.

1 Supported by Cofin grant from MIUR, Rome, to G.B.

2 Correspondence: Giovanna Berruti, Department of Biology, University of Milan, Via Celoria 26, 20133 Milano, Italy. FAX: 39 025 031 4802; giovanna.berruti{at}unimi.it






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Copyright © 2005 by the Society for the Study of Reproduction.