Cui Gaofeng, Jiang Zhiyan, Chen Yaoyao, Li Yun, Ai Shupei, Sun Ranran, Yi Xin, Zhong Guohua
College of Plant Protection, South China Agricultural University, Guangzhou 510642, China.
Guangdong Provincial Key Laboratory of Silviculture, Protection and Utilization, Guangdong Academy of Forestry, Guangzhou 510520, China.
iScience. 2023 Jun 7;26(7):107040. doi: 10.1016/j.isci.2023.107040. eCollection 2023 Jul 21.
Lysosome motility is critical for the cellular function. However, Rab7-related transport elements showed genetic differences between vertebrates and invertebrates, making the mechanism of lysosomal motility mysterious. We suggested that Rab7 interacted with RILP as a feature of highly evolved organisms since they could interact with each other in but not in . The N-terminus of Sf-RILP was identified to be necessary for their interaction, and Glu61 was supposed to be the key point for the stability of the interaction. A GC-rich domain on the C-terminal parts of Sf-RILP hampered the expression of Sf-RILP and its interaction with Sf-Rab7. Although the corresponding vital amino acids in the mammalian model at the C-terminus of Sf-RILP turned to be neutral, the C-terminus would also help with the homologous interactions between RILP fragments in insects. The significantly different interactions in invertebrates shed light on the biodiversity and complexity of lysosomal motility.
溶酶体运动对细胞功能至关重要。然而，Rab7相关的运输元件在脊椎动物和无脊椎动物之间表现出遗传差异，这使得溶酶体运动的机制变得神秘。我们认为，Rab7与RILP相互作用是高等生物的一个特征，因为它们在[具体物种1]中可以相互作用，但在[具体物种2]中则不能。Sf-RILP的N端被确定为它们相互作用所必需的，而Glu61被认为是相互作用稳定性的关键点。Sf-RILP C端部分富含GC的结构域阻碍了Sf-RILP的表达及其与Sf-Rab7的相互作用。尽管在哺乳动物模型中，Sf-RILP C端相应的关键氨基酸变为中性，但C端也有助于昆虫中RILP片段之间的同源相互作用。无脊椎动物中显著不同的相互作用揭示了溶酶体运动的生物多样性和复杂性。
