DSSylation, a novel guide for protein degradation?

Cheng-Xin Gong

doi:10.1007/s13238-014-0020-9

Abstract

DSSylation, a novel guide for protein degradation?

Highlights

There are many different posttranslational modifications of proteins, such as phosphorylation, acylation, methylation, glycosylation, glycation, truncation, ubiquitination, and oxidation. Some of these modifications are crucial for the maturation, proper folding, and biological activity of a protein, while others label a protein for degradation. In this issue of Protein & Cell, Zhang et al (2014) reported a novel posttranslational modification of protein, named DSSylation, by which a protein is conjugated with DSS1, a small and highly acidic and conserved protein encoded by the gene DSS1
The lack of this gene is found in patients with a dominantly inherited heterogeneous limb developmental disorder called ectrodactyly or split hand/split foot malformation type 1 (Crackower et al, 1996)
By using liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS), Zhang et al identified 39 proteins from DSS1 conjugates affinity-purified from the lysates of the cells after exposure with UV radiation

Summary

Introduction

There are many different posttranslational modifications of proteins, such as phosphorylation, acylation, methylation, glycosylation, glycation, truncation, ubiquitination, and oxidation. In this issue of Protein & Cell, Zhang et al (2014) reported a novel posttranslational modification of protein, named DSSylation, by which a protein is conjugated with DSS1, a small and highly acidic and conserved protein encoded by the gene DSS1 (deleted in split hand/split foot 1). Zhang et al demonstrated both in vitro and in cultured cells that DSS1 forms SDS-resistant adducts with cellular proteins.

Results

Conclusion