Evolutional insights into the interaction between Rab7 and RILP in lysosome motility

被引：1

作者：

Cui, Gaofeng ^{[1
,2
]}

Jiang, Zhiyan ^{[1
]}

Chen, Yaoyao ^{[1
]}

Li, Yun ^{[1
]}

Ai, Shupei ^{[1
]}

Sun, Ranran ^{[1
]}

Yi, Xin ^{[1
]}

Zhong, Guohua ^{[1
]}

机构：

[1] South China Agr Univ, Coll Plant Protect, Guangzhou 510642, Peoples R China

[2] Guangdong Acad Forestry, Guangdong Prov Key Lab Silviculture Protect & Util, Guangzhou 510520, Peoples R China

来源：

ISCIENCE | 2023年 / 26卷 / 07期

基金：

中国国家自然科学基金;

关键词：

MOLECULAR-DYNAMICS; HIGH-THROUGHPUT; HOPS COMPLEX; PROTEIN RILP; TRANSPORT; FUSION; RECRUITMENT; PREDICTION; AUTOPHAGY;

D O I：

10.1016/j.isci.2023.107040

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Lysosome motility is critical for the cellular function. However, Rab7-related transport elements showed genetic differences between vertebrates and inver-tebrates, 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 Spodoptera frugiperda but not in Drosophila melanogaster. 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 corre-sponding 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 inter-actions in invertebrates shed light on the biodiversity and complexity of lyso-somal motility.

引用

页数：22