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USP13 binds WWP1. 12 / 12
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"Immunoprecipitation with WWP1 antibody further validated the interaction between WWP1 and USP13 (Fig. 3B)."
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"Next, we transfected Myc-tagged WWP1 (Myc-WWP1), along with Flag-tagged USP13 (Flag-USP13) or an empty vector, into HCC and HEK293T cells, followed by a Co-IP assay to validate the binding between USP13 and WWP1."
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"Overall, there was an interaction between USP13 and WWP1."
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"Since our findings described above demonstrated the interaction between USP13 and WWP1, we wondered whether USP13 regulated WWP1 through deubiquitination."
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"According to our results, USP13 truncations containing either the N-terminal region (aa1–300 and aa1–624) or the C-terminal region (aa301–863 and aa625–863) could bind to WWP1."
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"Finally, our functional experiments in HCC cells and a subcutaneous xenograft model further revealed the oncogenic role of the USP13-WWP1 axis both in vitro and in vivo."
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"Furthermore, USP13 can interact with WWP1 and then remove the K29- and K48-linked polyubiquitination chains from WWP1 to stabilize the WWP1 protein via the ubiquitin–proteasome pathway."
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"USP13 interacted with WWP1 in HCC cells."
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"Immunoprecipitation with WWP1 antibody further validated the interaction between WWP1 and USP13 (Fig.  xref B)."
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"To determine the specific region of USP13 that interacts with WWP1, we constructed five Flag-tagged USP13 truncation plasmids."
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"Overall, there was an interaction between USP13 and WWP1."
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sparser
"Since our findings described above demonstrated the interaction between USP13 and WWP1, we wondered whether USP13 regulated WWP1 through deubiquitination."
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