IndraLab

Statements


USP15 activates TRIM25. 9 / 12
| 9

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"Ubiquitin specific peptidase 15 (USP15) could enhance the stabilization of TRIM25 by counteracting its K48 linked ubiquitylation and thereby positively regulate the TRIM25-RIG-I signaling pathway."

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"Furthermore, ectopic expression of USP15 enhanced the TRIM25- and RIG-I-dependent production of type I IFN and suppressed RNA virus replication."

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"Through a combination of biochemical and molecular assays, we further found that USP15 removed Lys 48 -linked ubiquitin moieties from TRIM25, thereby preventing TRIM25 degradation by the proteasome."

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"In addition, the ectopic expression of USP15 enhances the TRIM25- and RIG-I-mediated production of type I IFN and thus suppresses RNA virus replication, whereas the depletion of USP15 causes decreased IFN production and markedly enhanced viral replication (85)."

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"Our study also revealed some of the details about how and when during viral infection USP15 modulates TRIM25 activity."

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"USP15 deubiquitinates LUBACmediated K48-linked ubiquitination of TRIM25 and promotes the protein stability of TRIM25, there by promoting K63-linked ubiquitination of RIG-I and potentiating virus-triggered expression of type I IFN genes [82] ."

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"On the other hand, USP4 and USP15 enhance the stability of RIG-I and TRIM25, respectively, by proteolytically cleaving K48 linked ubiquitylation from these molecules XREF_BIBR, XREF_BIBR."

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"Ubiquitin specific protease 15 (USP15) prevents LUBAC-dependent degradation of TRIM25 which also promotes RIG-I signaling pathways [151]."
| PMC

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"In contrast, endogenous TRIM25 protein abundance did not change in USP15 expressing cells, suggesting that USP15 prevented the degradation of TRIM25."