Cloning of Schistosoma mansoni Seven in Absentia (SmSINA)+ homologue cDNA, a gene involved in ubiquitination of SmRXR1 and SmRXR2

Marcelo R. Fantappié, Ahmed Osman, Christer Ericsson, Edward G. Niles, Philip T. LoVerde

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

Drosophila (SINA) and human Seven in Absentia (SIAH-1 and SIAH-2) have been implicated in ubiquitin-mediated proteolysis of different target proteins. Using the Schistosoma mansoni nuclear receptor SmRXR2 as bait in a yeast two-hybrid system, we identified a DNA fragment that encodes part of the schistosome homologue of the Seven in Absentia protein (SmSINA). Screening of S. mansoni cDNA expression library resulted in the isolation of a cDNA containing the full-length coding region of SmSINA. SmSINA contains the characteristic structural features of other SINA proteins including a conserved N-terminal RING finger domain and a cysteine-rich C-terminus. We demonstrate that SmSINA associates with SmRXR2 and SmRXR1 both in vivo and in vitro, and define the binding domains in SmRXR2 and SmRXR1 that mediate their interaction. Schistosome SINA co-localizes with SmRXR2 and SmRXR1 in vitelline cells. In addition, we show that SmSINA stimulates the ubiquination of both SmRXR2 and SmRXR1 in vitro. Our findings suggest that SmSINA regulates ubiquitination and ubiquitin-induced degradation of schistosome nuclear receptors (RXR1 and RXR2) via the ubiquitin-proteasome pathway.

Original languageEnglish (US)
Pages (from-to)45-54
Number of pages10
JournalMolecular and Biochemical Parasitology
Volume131
Issue number1
DOIs
StatePublished - Sep 2003

Keywords

  • Proteasomal degradation
  • Retinoid X receptor
  • Schistosoma mansoni
  • Seven in Absentia
  • Ubiquitination

ASJC Scopus subject areas

  • Parasitology
  • Molecular Biology

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