Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2

Ester Zito, Alessandro Fraldi, Stefano Pepe, Ida Annunziata, Gary Kobinger, Paola Di Natale, Andrea Ballabio, Maria Pia Cosma

Research output: Contribution to journalArticlepeer-review


Sulphatases undergo a unique post-translational modification that converts a highly conserved cysteine located within their active site into formylglycine. This modification is necessary for the catalytic activities of the sulphatases, and it is generated by the protein product of sulphatase-modifying factor 1 (SUMF1), the gene mutated in multiple sulphatase deficiency (MSD). A paralogous gene, SUMF2, was discovered through its sequence similarity to SUMF1. We present evidence that SUMF2 colocalizes with SUMF1 within the endoplasmic reticulum and that the two proteins form heterodimers. SUMF1 and SUMF2 also form homodimers. In addition, SUMF2 is able to associate with the sulphatases with and without SUMF1. We have previously shown that co-transfection of SUMF1 with the sulphatase complementary DNAs greatly enhances the activities of the overexpressed sulphatases. Here, we show that SUMF2 inhibits the enhancing effects of SUMF1 on sulphatases, suggesting that the SUMF1-SUMF2 interaction represents a further level of control of these sulphatase activities.

Original languageEnglish (US)
Pages (from-to)655-660
Number of pages6
JournalEMBO reports
Issue number7
StatePublished - Jul 2005
Externally publishedYes


  • Enzymatic activity
  • Inborn errors of metabolism
  • Protein-protein interactions

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics


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