Faculty of Biotechnology, Department of Protein Engineering, University of Wroclaw, Joliot-Curie 14a, 50-383, Wroclaw, Poland.
Faculty of Biotechnology, Department of Protein Engineering, University of Wroclaw, Joliot-Curie 14a, 50-383, Wroclaw, Poland.
Cytokine Growth Factor Rev. 2021 Aug;60:89-106. doi: 10.1016/j.cytogfr.2021.03.004. Epub 2021 Mar 27.
Receptor tyrosine kinases (RTKs) constitute a large group of cell surface proteins that mediate communication of cells with extracellular environment. RTKs recognize external signals and transfer information to the cell interior, modulating key cellular activities, like metabolism, proliferation, motility, or death. To ensure balanced stream of signals the activity of RTKs is tightly regulated by numerous mechanisms, including receptor expression and degradation, ligand specificity and availability, engagement of co-receptors, cellular trafficking of the receptors or their post-translational modifications. One of the most widespread post-translational modifications of RTKs is glycosylation of their extracellular domains. The sugar chains attached to RTKs form a new layer of information, so called glyco-code that is read by galectins, carbohydrate binding proteins. Galectins are family of fifteen lectins implicated in immune response, inflammation, cell division, motility and death. The versatility of cellular activities attributed to galectins is a result of their high abundance and diversity of their cellular targets. A various sugar specificity of galectins and the differential ability of galectin family members to form oligomers affect the spatial distribution and the function of their cellular targets. Importantly, galectins and RTKs are tightly linked to the development, progression and metastasis of various cancers. A growing number of studies points on the close cooperation between RTKs and galectins in eliciting specific cellular responses. This review focuses on the identified complexes between galectins and RTK members and discusses their relevance for the cell physiology both in healthy tissues and in cancer.
受体酪氨酸激酶（RTKs）是一大类细胞表面蛋白，它们介导细胞与细胞外环境的通讯。RTKs 识别外部信号，并将信息传递到细胞内部，调节关键的细胞活动，如代谢、增殖、运动或死亡。为了确保信号的平衡流动，RTKs 的活性受到许多机制的严格调节，包括受体表达和降解、配体特异性和可用性、共受体的参与、受体的细胞内运输或其翻译后修饰。RTKs 的最广泛的翻译后修饰之一是其细胞外结构域的糖基化。与 RTKs 结合的糖链形成了一个新的信息层，即所谓的糖码，它被半乳糖凝集素（galectin），即碳水化合物结合蛋白读取。Galectin 是一个包含十五个凝集素的家族，参与免疫反应、炎症、细胞分裂、运动和死亡。Galectins 归因于其高丰度和细胞靶标的多样性而具有多种细胞活性。Galectins 的各种糖特异性和 galectin 家族成员形成寡聚体的不同能力影响其细胞靶标的空间分布和功能。重要的是，Galectin 和 RTKs 与各种癌症的发生、发展和转移密切相关。越来越多的研究指出 RTKs 和 galectin 之间在引发特定细胞反应方面的密切合作。本综述重点介绍了 galectin 和 RTK 成员之间已鉴定的复合物，并讨论了它们在健康组织和癌症中的细胞生理学中的相关性。
