Unit

UNIT 14.7 Tyrosine O-Sulfation

  1. Denis Corbeil,
  2. Christoph Thiele,
  3. Wieland B. Huttner

Published Online: 1 MAR 2005

DOI: 10.1002/0471140864.ps1407s39

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Corbeil, D., Thiele, C. and Huttner, W. B. 2005. Tyrosine O-Sulfation. Current Protocols in Protein Science. 39:14.7:14.7.1–14.7.14.

Author Information

  1. Max-Planck-Institute of Molecular Cell Biology and Genetics, Dresden, Germany

Publication History

  1. Published Online: 1 MAR 2005
  2. Published Print: FEB 2005

This is not the most recent version of the article. View current version (1 APR 2015)

Abstract

The O-sulfation of tyrosine residues of plasma membrane and secretory proteins that transit through the secretory pathway of eukaryotic cells is a widespread post-translational modification. This enzymatic reaction is catalyzed by trans-Golgi-associated tyrosylprotein sulfotransferases, which recognize tyrosine residues located in a specific acidic amino acid sequence. Tyrosine sulfation promotes extracellular protein–protein interactions involved in diverse biological processes, ranging from the receptor binding of regulatory peptides to the interaction of viral envelope proteins with the cell surface. This unit outlines procedures to determine whether a protein of interest contains sulfated tyrosine residues, using methods based on labeling proteins with inorganic [35S]-sulfate, alkaline hydrolysis, and one-dimensional thin-layer electrophoresis.

Keywords:

  • Sulfation;
  • tyrosine residue;
  • post-translational modification;
  • sulfate labeling