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. 2021 Mar 4;9:648024. doi: 10.3389/fcell.2021.648024

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Copyright © 2021 Yong, Mao, Shen, Zhang, Billadeau and Jia.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Legionella effector RidL directly binds the retromer subunit VPS29, outcompeting TBC1D5 and VARP binding. (A) Model depicting how RidL subverts retromer-dependent trafficking. Left: retromer mediates endosomes-to-plasma membrane trafficking, together with TBC1D5 and VARP. Right: Legionella employs type IV secretion systems (T4SSs) to translocate RidL and other effector proteins into host cells. RidL localizes on the LCV, probably via its ability to bind PtdIns(3)P. RidL directly binds to VPS29, and inhibits the binding of TBC1D5 or VARP to retromer. (B) Interaction between TBC1D5 (light blue) and VPS29 (green). (C) Interaction between VARP (hot pink) and VPS29 (green). (D) Interaction between RidL (cyan) and VPS29 (green). Inset shows alignment of VPS29-binding sequences from TBC1D5, VARP, and RidL.