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J Cancer 2018; 9(22):4128-4138. doi:10.7150/jca.26885 This issue Cite

Research Paper

Identification of Integrin β1 as a Novel PAG1-Interacting Protein Involved in the Inherent Radioresistance of Human Laryngeal Carcinoma

Xiaoxia Dong1, Zhiguo Luo2, Tiantian Liu2, Jingjing Chai2, Qing Ke2, Li Shen2✉

1. Department of pharmacology, School of Basic Medical Sciences, Hubei University of Medicine, Shiyan, Hubei 442000, P.R. China
2. Department of Clinical Oncology, Taihe Hospital, Hubei University of Medicine, Shiyan, Hubei 442000, P.R. China

✉ Corresponding author: Li Shen, Department of Clinical Oncology, Taihe Hospital, Hubei University of Medicine, 30 South Renmin Road, Shiyan, Hubei 442000, P.R.China. E-mail: shenlihbcom

Citation:
Dong X, Luo Z, Liu T, Chai J, Ke Q, Shen L. Identification of Integrin β1 as a Novel PAG1-Interacting Protein Involved in the Inherent Radioresistance of Human Laryngeal Carcinoma. J Cancer 2018; 9(22):4128-4138. doi:10.7150/jca.26885. https://www.jcancer.org/v09p4128.htm
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Abstract

Inherent radioresistance plays a crucial role in the failure of radiotherapy. Using the inherent radioresistant (Hep-2max) and radiosensitive (Hep-2min) cell lines established from the parental cell line Hep-2, we previously reported that phosphoprotein associated with glycosphingolipid-enriched microdomains 1(PAG1) overexpression in laryngeal carcinoma cells was correlated with inherent radioresistant phenotypes. However, the underlying mechanisms of this effect remain unknown. In the present study, we performed a proteomic screen to investigate the interactome of PAG1 in Hep-2max cells resulting in the identification of several interaction partners. Bioinformatic analysis and immunofluorescence experiments indicated the integrin β1 to be a crucial interaction partner of PAG1. PAG1 was also highly expressed in laryngeal carcinoma radioresistant tissues and showed co-localization with integrin β1. In addition, we demonstrated that integrin β1's binding to PAG1 could be interrupted by MβCD, an inhibitor of lipid rafts formation. Moreover, knockdown of integrin β1 by RNA interference sensitized radioresistant cells to irradiation. Importantly, we identified 2 potential interaction sites (Pro216-Arg232 and Asn356-Gly377) in the cytoplasmic domain of PAG1 using high throughput peptide arrays. Taken together, these results suggest that the binding of PAG1 to integrin β1 in lipid rafts is essential for inherent radioresistance of human laryngeal carcinoma.

Keywords: PAG1, integrin β1, inherent radioresistance, laryngeal carcinoma, interaction partner

Citation styles

APA
Dong, X., Luo, Z., Liu, T., Chai, J., Ke, Q., Shen, L. (2018). Identification of Integrin β1 as a Novel PAG1-Interacting Protein Involved in the Inherent Radioresistance of Human Laryngeal Carcinoma. Journal of Cancer, 9(22), 4128-4138. https://doi.org/10.7150/jca.26885.

ACS
Dong, X.; Luo, Z.; Liu, T.; Chai, J.; Ke, Q.; Shen, L. Identification of Integrin β1 as a Novel PAG1-Interacting Protein Involved in the Inherent Radioresistance of Human Laryngeal Carcinoma. J. Cancer 2018, 9 (22), 4128-4138. DOI: 10.7150/jca.26885.

NLM
Dong X, Luo Z, Liu T, Chai J, Ke Q, Shen L. Identification of Integrin β1 as a Novel PAG1-Interacting Protein Involved in the Inherent Radioresistance of Human Laryngeal Carcinoma. J Cancer 2018; 9(22):4128-4138. doi:10.7150/jca.26885. https://www.jcancer.org/v09p4128.htm

CSE
Dong X, Luo Z, Liu T, Chai J, Ke Q, Shen L. 2018. Identification of Integrin β1 as a Novel PAG1-Interacting Protein Involved in the Inherent Radioresistance of Human Laryngeal Carcinoma. J Cancer. 9(22):4128-4138.

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