The Arf GTPase family is involved in a wide range of cellular regulation including membrane trafficking and organelle–structure assembly. Here, we have generated a proximity interaction network for the Arf family using the miniTurboID approach combined with TMT-based quantitative mass spectrometry. Our interactome confirmed known interactions and identified many novel interactors that provide leads for defining Arf pathway cell biological functions. We explored the unexpected finding that phospholipase D1 (PLD1) preferentially interacts with two closely related but poorly studied Arf family GTPases, ARL11 and ARL14, showing that PLD1 is activated by ARL11/14 and may recruit these GTPases to membrane vesicles, and that PLD1 and ARL11 collaborate to promote macrophage phagocytosis. Moreover, ARL5A and ARL5B were found to interact with and recruit phosphatidylinositol 4-kinase beta (PI4KB) at trans-Golgi, thus promoting PI4KB's function in PI4P synthesis and protein secretion.

中文翻译：

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定义 Arf GTPases 的近端相互作用网络揭示了 PLD1 和 PI4KB 的调节机制

Arf GTPase 家族参与广泛的细胞调节，包括膜运输和细胞器结构组装。在这里，我们使用 miniTurboID 方法结合基于 TMT 的定量质谱法为 Arf 家族生成了邻近相互作用网络。我们的相互作用组证实了已知的相互作用，并鉴定了许多新的相互作用因子，为定义 Arf 通路细胞生物学功能提供了线索。我们探索了意想不到的发现，即磷脂酶 D1 (PLD1) 优先与两个密切相关但研究很少的 Arf 家族 GTP 酶 ARL11 和 ARL14 相互作用，表明 PLD1 被 ARL11/14 激活，并可能将这些 GTP 酶募集到膜囊泡，并且 PLD1 和ARL11 协同促进巨噬细胞的吞噬作用。此外，ARL5A和ARL5B被发现与反式高尔基体处的磷脂酰肌醇4激酶β（PI4KB）相互作用并募集，从而促进PI4KB在PI4P合成和蛋白质分泌中的功能。