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USP13 deubiquitinates PTEN. 18 / 19
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"In contrast, USP13 directly binds and deubiquitylates PTEN to suppress tumorigenesis and glycolysis in PTEN-positive breast cancer cells (35)."
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"Deubiquitylation and stabilization of PTEN by USP13."
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"In addition to its oncogenic roles, USP13 exerts a tumor-suppressive role by deubiquitinating PTEN in different types of cancers."
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"Wild-type USP13 purified from either bacteria or 293T cells, but not its catalytically inactive mutant C345A, decreased PTEN poly-ubiquitination by 64-70% in vitro (XREF_FIG)."
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"On the other hand, ectopic expression of wild-type USP13, but not the C345A mutant which is still capable of interacting with PTEN (XREF_FIG), reduced the poly-ubiquitination of PTEN by 65% (XREF_FIG), suggesting that the enzymatic activity of USP13 is indispensable for USP13 dependent deubiquitination of PTEN."
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"For example, USP13 prevents tumor cell growth by deubiquitinating PTEN in breast cancer, OSCC and bladder cancer."
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"Therefore, USP13 can directly deubiquitinate PTEN."
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"PTEN is deubiquitinated by USP13 in bladder cancer, and its stabilized expression suppresses tumor progression (127)."
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"PTEN is ubiquitinated by WWP2 and NEDD4 [ 49 , 50 ] and is deubiquitinated by USP13 and OTUD3 [ 19 , 20 ]."
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"Deubiquitination of PTEN by USP13, a deubiquitinating enzyme, stabilized PTEN, and thereby inhibited breast cancer tumorigenesis [5]."
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"USP13, another PTEN deubiquitinase, different with USP7-mediated deubiquitination of PTEN monoubiquitination, it reverses PTEN polyubiquitination, thus promoting the PTEN stabilization and tumor suppr[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In these tumors, USP13 interacts with and deubiquitinates the tumor suppressor PTEN protein, thereby stabilizing and increasing the expression of PTEN [16–18]."
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"Ubiquitin-specific peptidase 13 (USP13) can deubiquitinate the PTEN protein and stabilize it."
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"Our findings revealed that USP13 alleviates MASH by directly binding to and deubiquitinating PTEN."
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"The decreased expression of USP13 promoted PTEN ubiquitylation, leading to PTEN degradation, thereby contributing to fibroblast activation and pathogenesis of IPF [101]."
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"Deubiquitination and stabilization of PTEN by USP13."
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"USP13 deubiquitinates and stabilizes PTEN."
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"However, Zhang et al. revealed that USP13 can deubiquitinate and stabilize the PTEN protein, thus inhibiting the Akt pathway and suppressing breast cancer progression [18]."
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