Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID: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 cells. 1534 53

DNAJB13 is a type II HSP40/DnaJ protein. Using a specific antibody raised against the recombinant DNAJB13 protein, we characterized DNAJB13 in mouse testes and epididymal spermatozoa. The expression of DNAJB13 protein in testis was undetectable until postnatal Week 4 revealed by Western blot analysis, whereas Dnajb13 mRNA was detectable as early as postnatal Week 1 by RT-PCR. Immunohistochemistry analyses showed that DNAJB13 was localized in the cytoplasm of spermatids from step 2 to 3 onward with the strongest expression in step 9-10, and in the spermatid flagella. In mature spermatozoa, DNAJB13 was present along the entire length of the sperm flagellum, but not in the SDS-resistant tail structures lacking the flagellar axoneme, strongly suggesting that DNAJB13 is an axoneme-associated component. In addition, we showed that the expression of Dnajb13 mRNA and DNAJB13 protein was unaltered after heat shock treatment, indicating that DNAJB13 was constitutively expressed in mouse testis. Taken together, the present study suggested that DNAJB13 might be involved in assembly and stability of axoneme during sperm flagellum development.
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PMID:A heat-shock protein 40, DNAJB13, is an axoneme-associated component in mouse spermatozoa. 1824 31