التفاصيل البيبلوغرافية
| العنوان: |
SNX27-FERM-SNX1 complex structure rationalizes divergent trafficking pathways by SNX17 and SNX27. |
| المؤلفون: |
Xin Yong, Lin Zhao, Wenfeng Hu, Qingxiang Sun, Hyoungjun Ham, Zhe Liu, Jie Ren, Zhen Zhang, Yifei Zhou, Qin Yang, Xianming Mo, Junjie Hu, Billadeau, Daniel D., Da Jia |
| المصدر: |
Proceedings of the National Academy of Sciences of the United States of America; 9/7/2021, Vol. 118 Issue 36, p1-11, 11p |
| مصطلحات موضوعية: |
MEMBRANE proteins, NEURAL development, FREIGHT & freightage, ENDOSOMES |
| مستخلص: |
The molecular events that determine the recycling versus degradation fates of internalized membrane proteins remain poorly understood. Two of the three members of the SNX-FERM family, SNX17 and SNX31, utilize their FERM domain to mediate endocytic trafficking of cargo proteins harboring the NPxY/NxxY motif. In contrast, SNX27 does not recycle NPxY/NxxY-containing cargo but instead recycles cargo containing PDZ-binding motifs via its PDZ domain. The underlying mechanism governing this divergence in FERM domain binding is poorly understood. Here, we report that the FERM domain of SNX27 is functionally distinct from SNX17 and interacts with a novel DLF motif localized within the N terminus of SNX1/2 instead of the NPxY/NxxY motif in cargo proteins. The SNX27-FERM-SNX1 complex structure reveals that the DLF motif of SNX1 binds to a hydrophobic cave surrounded by positively charged residues on the surface of SNX27. The interaction between SNX27 and SNX1/2 is critical for efficient SNX27 recruitment to endosomes and endocytic recycling of multiple cargoes. Finally, we show that the interaction between SNX27 and SNX1/2 is critical for brain development in zebrafish. Altogether, our study solves a long-standing puzzle in the field and suggests that SNX27 and SNX17 mediate endocytic recycling through fundamentally distinct mechanisms. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
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