The ATP binding cassette (ABC) transporters, first discovered as high-affinity nutrient importers in bacteria, rose to prominence when their ability to confer multidrug resistance (MDR) to cancer cells was realized. The most characterized human permeability glycoprotein (P-gp) is a dominant exporter of anti-cancer drugs and its overexpression is directly linked to MDR. The overexpression of drug efflux pumps belonging to the ABC superfamily is also a frequent cause of resistance to antifungals. Fungi has a battery of ABC proteins, but in variable numbers and at different subcellular locations. These proteins perform many critical functions, from serving as gatekeepers for xenobiotic cleansing to translocating various structurally unrelated cargoes, including lipids, fatty acids, ions, peptides, sterols, metabolites and toxins. Their emerging additional roles in cellular physiology and virulence call for attention to analyze and re-examine their divergent functions in yeast. In brief, this review traces the history of ABC transporters in yeast and discusses their typical physiological functions that go beyond their well-known role as antifungal drug efflux pumps.

ATP 结合盒 (ABC) 转运蛋白最初是作为细菌中的高亲和力养分输入蛋白发现的，当它们赋予癌细胞多药耐药性 (MDR) 的能力被实现时，它就变得突出。最具特征的人类渗透性糖蛋白 (P-gp) 是抗癌药物的主要输出者，其过度表达与 MDR 直接相关。属于 ABC 超家族的药物外排泵的过度表达也是抗真菌药耐药的常见原因。真菌有一组 ABC 蛋白，但数量不同，位于不同的亚细胞位置。这些蛋白质执行许多关键功能，从充当异物清洁的看门人到转移各种结构无关的货物，包括脂质、脂肪酸、离子、肽、甾醇、代谢物和毒素。它们在细胞生理学和毒力中的新作用需要注意分析和重新检查它们在酵母中的不同功能。简而言之，这篇综述追溯了酵母中 ABC 转运蛋白的历史，并讨论了它们的典型生理功能，这些功能超出了它们作为抗真菌药物外排泵的众所周知的作用。