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. Author manuscript; available in PMC: 2024 Jan 5.
Published in final edited form as: Mol Cell. 2022 Dec 13:S1097-2765(22)01135-2. doi: 10.1016/j.molcel.2022.11.022

Figure 7: Model for LotA deubiquitinase activity.

Figure 7:

Secreted LotA localizes back to the cytosolic face of the LCV via the PI(3)P-binding LotAC domain. At the LCV, DUB activity of LotAM restricts long K48 and K63 polyUb. LotAN is kept inactive by a flexible A-UBD and inactive arrangement of the catalytic triad. Occupying a closed OTU:A-UBD conformation allows formation of an S1’ Ub-binding site. Binding of a K6-linked Ub into the S1’ site orients the LotAN catalytic triad, allowing for hydrolysis of K6 polyUb and prevention of VCP recruitment. Created with BioRender.com.