Citations 1
SNX27-FERM-SNX1 complex structure rationalizes divergent trafficking pathways by SNX17 and SNX27
Yong, Xin, Ham, Hyoungjun , Liu, Zhe , Ren, Jie , Zhang, Zhen , Zhou, Yifei, Yang, Qin , Mo, Xianming , Billadeau, Daniel D. , Jia, Da , Yang, Qin , Mo, Xianming , Hu, Junjie , Jia, Da , Yong, Xin, Zhao, Lin , Hu, Wenfeng , Sun, Qingxiang
Proceedings of the National Academy of Sciences | August 30, 2021 | Volume: 118 | Issue: 36 | Pages: No page available
Significance The sorting nexin proteins are critical for endosomal trafficking and signaling. SNX17 and SNX27 are two SNX proteins displaying high similarity in domain structure, including a common FERM domain; however, they mediate distinct endocytic recycling pathways. We now solve this mystery by demonstrating that the FERM domains of SNX17 and SNX27 have different functions. Whereas the FERM domain of SNX17 recognizes the NPxY/NxxY motif, the same domain in SNX27 binds to a novel “DLF” motif within the N termini of SNX1/2. The interaction between SNX27 and SNX1/2 not only helps efficient retrieval of multiple cargoes but also promotes endosomal recruitment of SNX27. We further demonstrate that the SNX27–SNX1/2 interaction is crucial to neuronal growth and brain development in zebrafish.