Tripartite motif-containing protein 6 facilitates growth and migration of breast cancer through degradation of STUB1

Proteins in the tripartite motif-containing protein (TRIM) family participates in carcinogenesis. However, little attention was focused on the role of TRIM6 on development of breast cancer. Expression level of TRIM6 was found to be markedly enhanced in breast cancer cells and tissues. Functional ass...

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Published inEuropean journal of histochemistry Vol. 65; no. 1
Main Authors Wei, Chuanchao, Wu, Jiayue, Liu, Weiyan, Lu, Jingfeng, Li, Hongchang, Hai, Benjun
Format Journal Article
LanguageEnglish
Published Italy PAGEPress Publications 10.03.2021
PAGEPress Scientific Publications, Pavia, Italy
PAGEPress Publications, Pavia, Italy
Subjects
Adaptor Proteins, Signal Transducing - metabolism
Animals
Breast cancer
Breast Neoplasms - metabolism
Breast Neoplasms - pathology
Cancer therapies
Carcinogenesis
Cell Line, Tumor
Cell Movement - physiology
Cell Proliferation - physiology
Degradation
Ethics
Female
Gene Expression Regulation, Neoplastic - physiology
Gene Knockdown Techniques
growth
Histology
Homology
Hospitals
Human subjects
Humans
Immunoprecipitation
Laboratory animals
Metastasis
Mice
Mice, Inbred BALB C
migration
Proteasomes
Proteins
Proteolysis
Signal Transduction - physiology
STUB1
Surgery
Therapeutic targets
Transcription Factors - metabolism
TRIM6
Tripartite Motif Proteins - genetics
Tripartite Motif Proteins - metabolism
Ubiquitin-Protein Ligases - genetics
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
YAP-Signaling Proteins
Yes-associated protein
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Summary:Proteins in the tripartite motif-containing protein (TRIM) family participates in carcinogenesis. However, little attention was focused on the role of TRIM6 on development of breast cancer. Expression level of TRIM6 was found to be markedly enhanced in breast cancer cells and tissues. Functional assays demonstrated that overexpression of TRIM6 promoted breast cancer progression through increase of YAP1 (Yes-associated Protein 1), while knockdown of TRIM6 suppressed in vitro breast cancer progression and in vivo tumor growth through decrease of YAP1. Co-Immunoprecipitation (co-IP) showed that TRIM6 interacted with STUB1 (stress induced phosphoprotein 1 homology and U-box containing protein 1). TRIM6 promoted ubiquitination-mediated degradation of STUB1 to promote YAP1 signaling. Overexpression of STUB1 attenuated TRIM6-induced promotion of breast cancer growth. In conclusion, TRIM6 contributed to breast cancer progression through ubiquitination-dependent proteasomal degradation of STUB1 and provocation of YAP1 pathway, providing potential therapeutic target for breast cancer.
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Availability of data and materials: All data generated or analyzed during this study are included in this published article.
Conflicts of interest: The authors state that there are no conflicts of interest to disclose.
Informed consent: Written informed consent was obtained from a legally authorized representative(s) for anonymized patient information to be published in this article.
Contributions: CW, JW, designed the study, supervised the data collection; WL, analyzed and interpreted the data; JL, HL, BH, prepared the manuscript for publication and reviewed the draft of the manuscript. All authors have read and approved the manuscript.
Ethics approval: All procedures performed in this study involving human participants were in accordance with the standards upheld by the Ethics Committee of Fudan-Minhang Academic Health System, Minhang Hospital, Fudan University and with those of the 1964 Helsinki Declaration and its later amendments for ethical research involving human subjects. All animal experiments were approved by the Ethics Committee of Fudan-Minhang Academic Health System, Minhang Hospital, Fudan University for the use of animals and conducted in accordance with the National Institutes of Health Laboratory Animal Care and Use Guidelines.
ISSN:1121-760X
2038-8306
2038-8306
DOI:10.4081/ejh.2021.3214