Abstract：
BACKGROUND: Sialylation of glycoproteins, including integrins, is crucial in various cancers and diseases such as immune disorders. These modifications significantly impact cellular functions and are associated with cancer progression. Sialylation, catalyzed by specific sialyltransferases (STs), has traditionally been considered to be regulated at the mRNA level.
METHODS: Recent research has expanded our understanding of sialylation, revealing ST activity changes beyond mRNA level variations. This includes insights into COPI vesicle formation and Golgi apparatus maintenance and identifying specific target proteins of STs that are not predictable through recombinant enzyme assays.
CONCLUSIONS: This review summarizes that Golgi-associated pathways largely influence the regulation of STs. GOLPH3, GORAB, PI4K, and FAK have become critical elements in sialylation regulation. Some STs have been revealed to possess specificity for specific target proteins, suggesting the presence of additional, enzyme-specific regulatory mechanisms.
CONCLUSIONS: This study enhances our understanding of the molecular interplay in sialylation regulation, mainly focusing on the role of integrin and FAK. It proposes a bidirectional system where sialylations might influence integrins and vice versa. The diversity of STs and their specific linkages offer new perspectives in cancer research, potentially broadening our understanding of cellular mechanisms and opening avenues for new therapeutic approaches in targeting sialylation pathways.
METHODS: Recent research has expanded our understanding of sialylation, revealing ST activity changes beyond mRNA level variations. This includes insights into COPI vesicle formation and Golgi apparatus maintenance and identifying specific target proteins of STs that are not predictable through recombinant enzyme assays.
CONCLUSIONS: This review summarizes that Golgi-associated pathways largely influence the regulation of STs. GOLPH3, GORAB, PI4K, and FAK have become critical elements in sialylation regulation. Some STs have been revealed to possess specificity for specific target proteins, suggesting the presence of additional, enzyme-specific regulatory mechanisms.
CONCLUSIONS: This study enhances our understanding of the molecular interplay in sialylation regulation, mainly focusing on the role of integrin and FAK. It proposes a bidirectional system where sialylations might influence integrins and vice versa. The diversity of STs and their specific linkages offer new perspectives in cancer research, potentially broadening our understanding of cellular mechanisms and opening avenues for new therapeutic approaches in targeting sialylation pathways.
摘要：
背景：糖蛋白的唾液酸化，包括整合素，在各种癌症和疾病如免疫疾病中至关重要。这些修饰显著影响细胞功能并且与癌症进展相关。唾液酸化,由特定的唾液酸转移酶（STs）催化，传统上被认为在mRNA水平上被调节。
方法：最近的研究扩大了我们对唾液酸化的理解，揭示ST活性变化超过mRNA水平变化。这包括对COPI囊泡形成和高尔基体维持的见解，以及鉴定通过重组酶测定无法预测的ST的特定靶蛋白。
结论：这篇综述总结了高尔基体相关通路在很大程度上影响STs的调节。GOLPH3GORAB,PI4K,和FAK已成为唾液酸化调节的关键元素。一些STs已被发现对特定靶蛋白具有特异性，暗示额外的存在，酶特异性调节机制。
结论：这项研究增强了我们对唾液酸化调节中分子相互作用的理解，主要集中在整合素和FAK的作用。它提出了一个双向系统，唾液酸化可能会影响整合素，反之亦然。STs的多样性及其特定的联系为癌症研究提供了新的视角，可能扩大我们对细胞机制的理解，并为靶向唾液酸化途径的新治疗方法开辟了途径。
方法：最近的研究扩大了我们对唾液酸化的理解，揭示ST活性变化超过mRNA水平变化。这包括对COPI囊泡形成和高尔基体维持的见解，以及鉴定通过重组酶测定无法预测的ST的特定靶蛋白。
结论：这篇综述总结了高尔基体相关通路在很大程度上影响STs的调节。GOLPH3GORAB,PI4K,和FAK已成为唾液酸化调节的关键元素。一些STs已被发现对特定靶蛋白具有特异性，暗示额外的存在，酶特异性调节机制。
结论：这项研究增强了我们对唾液酸化调节中分子相互作用的理解，主要集中在整合素和FAK的作用。它提出了一个双向系统，唾液酸化可能会影响整合素，反之亦然。STs的多样性及其特定的联系为癌症研究提供了新的视角，可能扩大我们对细胞机制的理解，并为靶向唾液酸化途径的新治疗方法开辟了途径。
