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

Abstract:

: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.

journal_name

EMBO Rep

journal_title

EMBO reports

authors

Zito E,Fraldi A,Pepe S,Annunziata I,Kobinger G,Di Natale P,Ballabio A,Cosma MP

doi

10.1038/sj.embor.7400454

keywords:

subject

Has Abstract

pub_date

2005-07-01 00:00:00

pages

655-60

issue

7

eissn

1469-221X

issn

1469-3178

pii

7400454

journal_volume

6

pub_type

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