[논문]DDIAS promotes STAT3 activation by preventing STAT3 recruitment to PTPRM in lung cancer cells

Im, Joo-Young; Kim, Bo-Kyung; Lee, Kang-Woo; Chun, So-Young; Kang, Mi-Jung; Won, Misun

doi:10.1038/s41389-019-0187-2

[해외논문] DDIAS promotes STAT3 activation by preventing STAT3 recruitment to PTPRM in lung cancer cells 원문보기

Oncogenesis, v.9 no.1, 2020년, pp.1 -

Im, Joo-Young (Personalized Genomic Medicine Research Center, KRIBB, Daejeon, 34141 Korea) , Kim, Bo-Kyung (Personalized Genomic Medicine Research Center, KRIBB, Daejeon, 34141 Korea) , Lee, Kang-Woo (Department of Oriental Medicine, Daejeon University, Daehak-ro 62, Dong-gu, Daejeon, 34520 South Korea) , Chun, So-Young (Personalized Genomic Medicine Research Center, KRIBB, Daejeon, 34141 Korea) , Kang, Mi-Jung (Personalized Genomic Medicine Research Center, KRIBB, Daejeon, 34141 Korea) , Won, Misun (Personalized Genomic Medicine Research Center, KRIBB, Daejeon, 34141 Korea)

Abstract ▼ AI-Helper

DNA damage-induced apoptosis suppressor (DDIAS) regulates cancer cell survival. Here we investigated the involvement of DDIAS in IL-6–mediated signaling to understand the mechanism underlying the role of DDIAS in lung cancer malignancy. We showed that DDIAS promotes tyrosine phosphorylation of signal transducer and activator of transcription 3 (STAT3), which is constitutively activated in malignant cancers. Interestingly, siRNA protein tyrosine phosphatase (PTP) library screening revealed protein tyrosine phosphatase receptor mu (PTPRM) as a novel STAT3 PTP. PTPRM knockdown rescued the DDIAS-knockdown-mediated decrease in STAT3 Y705 phosphorylation in the presence of IL-6. However, PTPRM overexpression decreased STAT3 Y705 phosphorylation. Moreover, endogenous PTPRM interacted with endogenous STAT3 for dephosphorylation at Y705 following IL-6 treatment. As expected, PTPRM bound to wild-type STAT3 but not the STAT3 Y705F mutant. PTPRM dephosphorylated STAT3 in the absence of DDIAS, suggesting that DDIAS hampers PTPRM/STAT3 interaction. In fact, DDIAS bound to the STAT3 transactivation domain (TAD), which competes with PTPRM to recruit STAT3 for dephosphorylation. Thus we show that DDIAS prevents PTPRM/STAT3 binding and blocks STAT3 Y705 dephosphorylation, thereby sustaining STAT3 activation in lung cancer. DDIAS expression strongly correlates with STAT3 phosphorylation in human lung cancer cell lines and tissues. Thus DDIAS may be considered as a potential biomarker and therapeutic target in malignant lung cancer cells with aberrant STAT3 activation.

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