Abstract
Ubiquitination is essential for various biological processes, such as signal transduction, intracellular traffick-ing, and protein degradation. Accumulating evidence has demonstrated that ubiquitination plays a crucial role in cancer development. In this report, we examine the expression and function of ubiquitin-conjugating enzyme E2S (UBE2S) in breast cancer. Immunohistochemical analysis revealed that UBE2S is highly expressed in breast cancer. The depletion of UBE2S by siRNA induced disruption of the actin cytoskel-eton and focal adhesions. Interestingly, phosphorylation of FAK at Tyr397, which is important for the transduction of integrin-mediated signaling, was significantly reduced by UBE2S knockdown. We also show that UBE2S knockdown suppressed the malignant characteristics of breast cancer cells, such as migration, invasion, and anchorage-independent growth. Our results indicate that UBE2S could be a potential target for breast cancer treatment.
Original language | English |
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Pages (from-to) | 763-772 |
Number of pages | 10 |
Journal | Tumor Biology |
Volume | 37 |
Issue number | 1 |
DOIs | |
Publication status | Published - 6 Aug 2015 |
Externally published | Yes |
Bibliographical note
Publisher Copyright:© 2015, International Society of Oncology and BioMarkers (ISOBM).
Keywords
- Anoikis
- Breast cancer
- FAK
- Invasion
- Migration
- UBE2S
- Ubiquitination