The SAC1 phosphatase domain of synaptojanin-1 is activated by interacting with polyunsaturated fatty acid-containing phosphatidic acids,FEBS Letters

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The SAC1 phosphatase domain of synaptojanin-1 is activated by interacting with polyunsaturated fatty acid-containing phosphatidic acids
FEBS Letters ( IF 3.0 ) Pub Date : 2021-08-13 , DOI: 10.1002/1873-3468.14177
Fumi Hoshino ₁ , Fumio Sakane ₁

Affiliation

Although there are many phosphatidic acid (PA) molecular species based on its fatty acyl compositions, their interacting partners have been poorly investigated. Here, we identified synaptojanin-1 (SYNJ1), Parkinson’s disease-related protein that is essential for regulating clathrin-mediated synaptic vesicle endocytosis via dually dephosphorylating D5 and D4 position phosphates from phosphatidylinositol (PI) (4,5)-bisphosphate, as a 1-stearoyl-2-docosahexaenoyl (18:0/22:6)-PA-binding protein. SYNJ1 failed to substantially associate with other acidic phospholipids. Although SYNJ1 interacted with 18:0/20:4-PA in addition to 18:0/22:6-PA, the association of the enzyme with 16:0/16:0-, 16:0/18:1-, 18:0/18:0-, or 18:1/18:1-PA was not considerable. 18:0/20:4- and 18:0/22:6-PAs bound to SYNJ1 via its SAC1 domain, which preferentially hydrolyses D4 position phosphate. Moreover, 18:0/20:4- and 18:0/22:6-PA selectively enhanced the D4-phosphatase activity, but not the D5-phosphatase activity, of SYNJ1.

中文翻译：

synaptojanin-1 的 SAC1 磷酸酶结构域通过与含多不饱和脂肪酸的磷脂酸相互作用而被激活

尽管根据其脂肪酰基组成有许多磷脂酸 (PA) 分子种类，但它们的相互作用伙伴的研究却很少。在这里，我们鉴定了 synaptojanin-1 (SYNJ1)，这是一种与帕金森病相关的蛋白质，它对于通过磷脂酰肌醇 (PI) (4,5)-二磷酸酯的 D5 和 D4 位磷酸盐双重去磷酸化来调节网格蛋白介导的突触小泡内吞作用至关重要。 1-硬脂酰-2-二十二碳六烯酰 (18:0/22:6)-PA 结合蛋白。 SYNJ1 未能与其他酸性磷脂显着结合。尽管 SYNJ1 除了 18:0/22:6-PA 之外还与 18:0/20:4-PA 相互作用，但该酶与 16:0/16:0-、16:0/18:1- 的关联， 18:0/18:0-或18:1/18:1-PA并不重要。 18:0/20:4- 和 18:0/22:6-PA 通过其 SAC1 结构域与 SYNJ1 结合，优先水解 D4 位磷酸盐。此外，18:0/20:4-和18:0/22:6-PA选择性增强SYNJ1的D4-磷酸酶活性，但不增强SYNJ1的D5-磷酸酶活性。

更新日期：2021-10-12

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