Department of Chemistry, Graduate School of Science, Chiba University, Japan.
Institute for Advanced Academic Research, Chiba University, Japan.
FEBS Open Bio. 2023 Jul;13(7):1333-1345. doi: 10.1002/2211-5463.13628. Epub 2023 May 21.
We previously reported that diacylglycerol (DG) kinase (DGK) δ interacts with DG-generating sphingomyelin synthase (SMS)-related protein (SMSr), but not SMS1 or SMS2, via their sterile α motif domains (SAMDs). However, it remains unclear whether other DGK isozymes interact with SMSs. Here, we found that DGKζ, which does not contain SAMD, interacts with SMSr and SMS1, but not SMS2. Deletion mutant analyses demonstrated that SAMD in the N-terminal cytosolic region of SMSr binds to the N-terminal half catalytic domain of DGKζ. However, the C-terminal cytosolic region of SMS1 interacts with the catalytic domain of DGKζ. Taken together, these results indicate that DGKζ associates with SMSr and SMS1 in different manners and suggest that they compose new DG signaling pathways.
我们之前报道过二酰基甘油 (DG) 激酶 (DGK) δ 通过其无活性 α 基序域 (SAMD) 与生成 DG 的鞘磷脂合酶 (SMS)-相关蛋白 (SMSr) 而不是 SMS1 或 SMS2 相互作用。然而，目前尚不清楚其他 DGK 同工酶是否与 SMSs 相互作用。在这里，我们发现不含 SAMD 的 DGKζ 与 SMSr 和 SMS1 相互作用，但不与 SMS2 相互作用。缺失突变分析表明，SMSr 细胞质 N 端区域的 SAMD 与 DGKζ 的 N 端半催化结构域结合。然而，SMS1 的细胞质 C 端区域与 DGKζ 的催化结构域相互作用。综上所述，这些结果表明 DGKζ 以不同的方式与 SMSr 和 SMS1 结合，并提示它们组成新的 DG 信号通路。
