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Int J Biol Sci 2023; 19(11):3324-3340. doi:10.7150/ijbs.80979 This issue Cite

Research Paper

SMURF2 facilitates ubiquitin-mediated degradation of ID2 to attenuate lung cancer cell proliferation

Mingwei Han#, Yixiao Guo#, Yiming Li#, Qingmei Zeng, Wanwan Zhu, Jianli Jiang✉

National Translational Science Center for Molecular Medicine and Department of Cell Biology, Fourth Military Medical University, Xi'an 710032, Shaanxi, China
# Equal contribution

✉ Corresponding author: Jianli Jiang, National Translational Science Center for Molecular Medicine and Department of Cell Biology, Fourth Military Medical University, Xi'an 710032, China. Email: jiangjledu.cn

Citation:
Han M, Guo Y, Li Y, Zeng Q, Zhu W, Jiang J. SMURF2 facilitates ubiquitin-mediated degradation of ID2 to attenuate lung cancer cell proliferation. Int J Biol Sci 2023; 19(11):3324-3340. doi:10.7150/ijbs.80979. https://www.ijbs.com/v19p3324.htm
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Abstract

Graphic abstract

SMAD-specific E3 ubiquitin protein ligase 2 (SMURF2) functions as either a tumor promoter or tumor suppressor in several tumors. However, the detailed effect of SMURF2 on non-small cell lung cancer has not been fully understood. In this study, SMURF2 expression and its diagnostic value were analyzed. Co-Immunoprecipitation (Co-IP), proximity ligation assay (PLA), chromatin immunoprecipitation (ChIP) and nude mice tumor-bearing model were applied to further clarify the role of SMURF2 in lung cancer. SMURF2 expression was reduced in the tumor tissues of patients with NSCLC and high SMURF2 expression was significantly correlated with favorable outcomes. Furthermore, the overexpression of SMURF2 significantly inhibited lung cancer cell progression. Mechanistically, SMURF2 interacted with inhibitor of DNA binding 2 (ID2), subsequently promoting the poly-ubiquitination and degradation of ID2 through the ubiquitin-proteasome pathway. Downregulated ID2 in lung cells dissociates endogenous transcription factor E2A, a positive regulator of the cyclin-dependent kinase inhibitor p21, and finally induces G1/S arrest in lung cancer cells. This study revealed that the manipulation of ID2 via SMURF2 may control tumor progression and contribute to the development of novel targeted antitumor drugs.

Keywords: non-small cell lung cancer, SMURF2, post-translational modifications, cell cycle, tumor progression

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APA
Han, M., Guo, Y., Li, Y., Zeng, Q., Zhu, W., Jiang, J. (2023). SMURF2 facilitates ubiquitin-mediated degradation of ID2 to attenuate lung cancer cell proliferation. International Journal of Biological Sciences, 19(11), 3324-3340. https://doi.org/10.7150/ijbs.80979.

ACS
Han, M.; Guo, Y.; Li, Y.; Zeng, Q.; Zhu, W.; Jiang, J. SMURF2 facilitates ubiquitin-mediated degradation of ID2 to attenuate lung cancer cell proliferation. Int. J. Biol. Sci. 2023, 19 (11), 3324-3340. DOI: 10.7150/ijbs.80979.

NLM
Han M, Guo Y, Li Y, Zeng Q, Zhu W, Jiang J. SMURF2 facilitates ubiquitin-mediated degradation of ID2 to attenuate lung cancer cell proliferation. Int J Biol Sci 2023; 19(11):3324-3340. doi:10.7150/ijbs.80979. https://www.ijbs.com/v19p3324.htm

CSE
Han M, Guo Y, Li Y, Zeng Q, Zhu W, Jiang J. 2023. SMURF2 facilitates ubiquitin-mediated degradation of ID2 to attenuate lung cancer cell proliferation. Int J Biol Sci. 19(11):3324-3340.

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