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USP15 stabilizes MDM2 to mediate cancer-cell survival and inhibit antitumor T cell responses
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USP15 stabilizes MDM2 to mediate cancer-cell survival and inhibit antitumor T cell responses
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Journal Article
USP15 stabilizes MDM2 to mediate cancer-cell survival and inhibit antitumor T cell responses
2014
Overview
Sun and colleagues show that the deubiquitinase USP15 stabilizes expression of the E3 ubiquitin ligase MDM2 in T cells, which results in inhibition of T cell activation, and in cancer cells, which results in survival of cancer cells.
Deubiquitinases (DUBs) are a new class of drug targets, although the physiological function of only few DUBs has been characterized. Here we identified the DUB USP15 as a crucial negative regulator of T cell activation. USP15 stabilized the E3 ubiquitin ligase MDM2, which in turn negatively regulated T cell activation by targeting the degradation of the transcription factor NFATc2. USP15 deficiency promoted T cell activation
in vitro
and enhanced T cell responses to bacterial infection and tumor challenge
in vivo
. USP15 also stabilized MDM2 in cancer cells and regulated p53 function and cancer-cell survival. Our results suggest that inhibition of USP15 may both induce tumor cell apoptosis and boost antitumor T cell responses.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ 96
/ 96/109
/ 96/31
/ Animals
/ Cell Differentiation - immunology
/ Humans
/ Listeria monocytogenes - immunology
/ Lymphocyte Activation - immunology
/ Melanoma, Experimental - immunology
/ Mice
/ NFATC Transcription Factors - metabolism
/ Proto-Oncogene Proteins c-mdm2 - genetics
/ Proto-Oncogene Proteins c-mdm2 - immunology
/ T cells
/ Tumor Suppressor Protein p53 - immunology
/ Tumors
/ Ubiquitin-Specific Proteases - genetics
