生物
信号转导衔接蛋白
高尔基体
AP-1转录因子
辅因子
细胞生物学
血浆蛋白结合
功能(生物学)
蛋白质靶向
保守序列
结合位点
酵母
膜蛋白
生物化学
肽序列
基因
转录因子
信号转导
膜
酶
内质网
作者
Lucas J. Marmorale,Huan Jin,Thomas G. Reidy,Brandon Palomino-Alonso,Christopher J. Zysnarski,Fatima Jordan-Javed,S. C. Lahiri,Mara C. Duncan
标识
DOI:10.1083/jcb.202309047
摘要
The highly conserved HEATR5 proteins are best known for their roles in membrane traffic mediated by the adaptor protein complex-1 (AP1). HEATR5 proteins rely on fast-evolving cofactors to bind to AP1. However, how HEATR5 proteins interact with these cofactors is unknown. Here, we report that the budding yeast HEATR5 protein, Laa1, functions in two biochemically distinct complexes. These complexes are defined by a pair of mutually exclusive Laa1-binding proteins, Laa2 and the previously uncharacterized Lft1/Yml037c. Despite limited sequence similarity, biochemical analysis and structure predictions indicate that Lft1 and Laa2 bind Laa1 via structurally similar mechanisms. Both Laa1 complexes function in intra-Golgi recycling. However, only the Laa2–Laa1 complex binds to AP1 and contributes to its localization. Finally, structure predictions indicate that human HEATR5 proteins bind to a pair of fast-evolving interacting partners via a mechanism similar to that observed in yeast. These results reveal mechanistic insight into how HEATR5 proteins bind their cofactors and indicate that Laa1 performs functions besides recruiting AP1.
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