Stone Martin J, Chuang Sara, Hou Xu, Shoham Menachem, Zhu John Z
Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia
N Biotechnol. 2009 Jun;25(5):299-317. doi: 10.1016/j.nbt.2009.03.011.
The post-translational sulfation of tyrosine residues occurs in numerous secreted and integral membrane proteins and, in many cases, plays a crucial role in controlling the interactions of these proteins with physiological binding partners as well as invading pathogens. Recent advances in our understanding of protein tyrosine sulfation have come about owing to the cloning of two human tyrosylprotein sulfotransferases (TPST-1 and TPST-2), the development of novel analytical and synthetic methodologies and detailed studies of proteins and peptides containing sulfotyrosine residues. In this article, we describe the TPST enzymes, review the major techniques available for studying the presence, location and function of tyrosine sulfation in proteins and discuss the biological functions and biochemical interactions of several proteins (or protein families) in which tyrosine sulfation influences the protein function. In particular, we describe the detailed evidence supporting the importance of tyrosine sulfation in the cellular adhesion function of P-selectin glycoprotein ligand-1, the leukocyte trafficking and pathogen invasion functions of chemokine receptors and the ligand binding and activation of other G-protein-coupled receptors by complement proteins, phospholipdis and glycoprotein hormones.
酪氨酸残基的翻译后硫酸化发生在众多分泌蛋白和整合膜蛋白中，并且在许多情况下，对于控制这些蛋白与生理结合伴侣以及入侵病原体之间的相互作用起着关键作用。由于两种人酪氨酸蛋白硫酸转移酶（TPST-1和TPST-2）的克隆、新型分析和合成方法的发展以及对含硫酸化酪氨酸残基的蛋白质和肽的详细研究，我们对蛋白质酪氨酸硫酸化的理解取得了最新进展。在本文中，我们描述了TPST酶，回顾了用于研究蛋白质中酪氨酸硫酸化的存在、位置和功能的主要技术，并讨论了几种蛋白质（或蛋白质家族）的生物学功能和生化相互作用，其中酪氨酸硫酸化影响蛋白质功能。特别是，我们描述了详细证据，支持酪氨酸硫酸化在P-选择素糖蛋白配体-1的细胞粘附功能、趋化因子受体的白细胞运输和病原体入侵功能以及补体蛋白、磷脂和糖蛋白激素对其他G蛋白偶联受体的配体结合和激活中的重要性。
