IndraLab

Statements

USP15 binds cGAS. 11 / 11
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sparser
"To identify the domains that are essential in the cGAS–USP15 interaction."
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"USP15 interacts with cGAS."
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"To confirm a direct interaction between cGAS and USP15, we performed GST pull-down experiments using recombinant GST-tagged cGAS and USP15 ( xref )."
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"We found that the two DUB domains and the linker region were necessary for USP15 interaction with cGAS (Figure xref , xref )."
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"Consistently, GST-tagged USP15 (521–981) pulled down recombinant cGAS (Figure xref ), indicating a direct interaction between USP15 and cGAS."
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"We also conducted a GST pull-down assay and found that deletion of the IDR completely abolished the interaction between cGAS and USP15, indicating that the IDR of USP15 was important for its direct binding with cGAS ( xref )."
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"To confirm that USP15 interacts with cGAS, we overexpressed Flag-epitope tagged USP15 and Myc epitope-tagged cGAS and performed co-IP experiments."
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"Although the direct interaction between cGAS and USP15 was abolished in the GST pull-down assay, their interaction remained to some extent after the IDR of USP15 was deleted in the co-IP assay, indicating the indirect interaction between cGAS and USP15 in cells, which might be responsible for the process of cGAS deubiquitylation by USP15 ( xref )."
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"In the resting state, USP15 interacts with cGAS, promoting its dimerization and phase separation through multivalent interactions."
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"Consistently, the interaction between cGAS and USP15 became weaker after the IDR of USP15 was deleted ( xref )."
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"Taken together, these results suggest that USP15 physically interacts with cGAS."
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