期刊
FEBS LETTERS
卷 595, 期 19, 页码 2479-2492出版社
WILEY
DOI: 10.1002/1873-3468.14177
关键词
docosahexaenoic acid; Parkinson's disease; phosphatidic acid; phosphatidylinositol 4-monophosphate; polyunsaturated fatty acid; SAC1 domain; synaptojanin-1
资金
- MEXT/JSPS (KAKENHI) [17H03650, 20H03205, 20J21133]
- Japan Food Chemical Research Foundation
- SENSHIN Medical Research Foundation
- Uehara Memorial Foundation
- Grants-in-Aid for Scientific Research [20H03205, 20J21133] Funding Source: KAKEN
The interaction between different molecular species of phosphatidic acid (PA) and SYNJ1 protein was investigated, revealing that 18:0/20:4- and 18:0/22:6-PA could bind to SYNJ1 through its SAC1 domain and enhance its D4-phosphatase activity.
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.
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