Cited by 93

Mechanism of cargo recognition by retromer-linked SNX-BAR proteins

Yong, Xin, Zhao, Lin, Deng, Wankun, Sun, Hongbin, Zhou, Xue, Mao, Lejiao, Hu, Wenfeng, Shen, Xiaofei, Sun, Qingxiang, Billadeau, Daniel D., Xue, Yu, Jia, Da·2020·PLOS Biology

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Crossref · 10.1371/journal.pbio.3000631

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  • Various sorting nexin proteins, such as SNX27, SNX32, SNX1-SNX6, and SNX1-SNX5, are autoinhibited in the basal state, with cargo binding enhancing their association with Retromer or membranes.

    “Interestingly, various sorting nexin proteins, such as SNX2729, SNX326,39, SNX1-SNX628, and SNX1-SNX540, operate similarly, being autoinhibited in the basal state, with cargo binding enhancing their association with Retromer or membranes.”

    From Structural basis for Retriever-SNX17 assembly and endosomal sorting (2024) · cites this paper as [28]

    The Results ('Identification of the SBM'; page unavailable) report that cargo and a membrane lipid cooperate to increase recruitment of the SNX1/SNX6 complex to liposomes. Another Results section ('Discovery and verification of additional SNX-BAR ligands'; page unavailable) shows cargo binding to SNX1/SNX5. Our copy does not establish basal-state autoinhibition of SNX1/SNX5 or the other listed proteins, or show cargo-enhanced Retromer association for them. (LLM, conf=0.83)

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Cited by

Sorted by citations

Authors
Yong, X., Zhao, L., Deng, W., Sun, H., Zhou, X., Mao, L., Hu, W., Shen, X., Sun, Q., Billadeau, D. D., Xue, Y., & Jia, D.
Venue
PLOS Biology
Published
2020-03-09
Volume
18
Issue
3
Pages
e3000631
ISSN
1545-7885
Cited by
93
References
3
Language
en
Funders
  • National Natural Science Foundation of China (#91854121, #31871429, #31671477)
  • Department of Science and Technology of Sichuan Province (2018RZ0128)
  • National Institutes of Health (NIDDK R01DK107733)
  • National Basic Research Program of China (2018YFC1005004)

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