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.

中文翻译：

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酪氨酸硫酸化：一种越来越被认可的分泌蛋白的翻译后修饰

酪氨酸残基的翻译后硫酸化发生在许多分泌的和完整的膜蛋白中，在许多情况下，在控制这些蛋白质与生理结合伙伴的相互作用以及入侵病原体方面起着至关重要的作用。由于克隆了两种人类酪氨酸蛋白磺基转移酶（TPST-1 和 TPST-2）、新的分析和合成方法的发展以及对含有磺基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，回顾了可用于研究存在的主要技术，酪氨酸硫酸化在蛋白质中的位置和功能，并讨论酪氨酸硫酸化影响蛋白质功能的几种蛋白质（或蛋白质家族）的生物学功能和生化相互作用。特别是，我们描述了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其他 G 蛋白的配体结合和活化中的重要性的详细证据。通过补体蛋白、磷脂和糖蛋白激素偶联受体。