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Genome Biol. 2001;2(10):RESEARCH0043. Epub 2001 Sep 13.

Characterization of alternatively spliced products and tissue-specific isoforms of USP28 and USP25.

Author information

  • 1Departament de Genètica, Facultat de Biologia, Universitat de Barcelona, Av Diagonal 645, 08028 Barcelona, Spain. gemma@porthos.bio.ub.es

Abstract

BACKGROUND:

The ubiquitin-dependent protein degradation pathway is essential for the proteolysis of intracellular proteins and peptides. Deubiquitinating enzymes constitute a complex protein family involved in a multitude of cellular processes. The ubiquitin-specific proteases (UBP) are a group of enzymes whose predicted function is to reverse the ubiquitinating reaction by removing ubiquitin from a large variety of substrates. We have lately reported the characterization of human USP25, a specific-ubiquitin protease gene at 21q11.2, with a specific pattern of expression in murine fetal brains and adult testis.

RESULTS:

Database homology searches at the DNA and protein levels and cDNA library screenings led to the identification of a new UBP member in the human genome, named USP28, at 11q23. This novel gene showed preferential expression in heart and muscle. Moreover, cDNA, expressed sequence tag and RT-PCR analyses provided evidence for alternatively spliced products and tissue-specific isoforms. Concerning function, USP25 overexpression in Down syndrome fetal brains was shown by real-time PCR.

CONCLUSIONS:

On the basis of the genomic and protein sequence as well as the functional data, USP28 and USP25 establish a new subfamily of deubiquitinating enzymes. Both genes have alternatively spliced exons that could generate protein isoforms with distinct tissue-specific activity. The overexpression of USP25 in Down syndrome fetal brains supports the gene-dosage effects suggested for other UBP members related to aneuploidy syndromes.

PMID:
11597335
[PubMed - indexed for MEDLINE]
PMCID:
PMC57798
Free PMC Article

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