Abstract
SCY1-like 1-binding protein 1 (SCYL1BP1) is a newly identified transcriptional activator domain containing protein with many unknown biological functions. Recently emerging evidence has revealed that it is a novel regulator of the p53 pathway, which is very important for the development of human cancer. However, the effects of SCYL1BP1 on human lung squamous carcinoma cell biological behavior remain poorly understood. In this study, we present evidence that SCYL1BP1 can promote the degradation of MDM2 protein and further inhibit the G1/S transition of lung squamous carcinoma cell lines. Functional assays found that reintroduction of SCYL1BP1 into lung squamous carcinoma cell lines significantly inhibited cell proliferation, migration, invasion and tumor formation in nude mice, suggesting strong tumor suppressive function of SCYL1BP1 in lung squamous carcinoma. Taken together, our data suggest that the interaction of SCYL1BP1/MDM2 could accelerate MDM2 degradation, and may function as an important tumor suppressor in lung squamous carcinomas.
Highlights
Murine double minute 2 (MDM2) is involved in cell growth and differentiation through its interaction with other cellular proteins (Uldrijan et al, 2007; Wang et al, 2009)
Our results showed that the growth of tumors from SCYL1BP1-upregulated xenografts was significantly inhibited when compared with that of tumors formed from control xenografts: 488.2±47.26 mm3 versus 919.9±75.73 mm3 of NCI-H226 cells (p=0.0013); 585.4±54.85 mm3 versus 921.9±80.04 mm3 of LTEP-S cells (p=0.0085), respectively (Figure 4A and 4B)
SCYL1BP1 was initially identified as an SCYL1binding protein (Di et al, 2003; Liu et al, 2012), but little is known about its biological function in human lung squamous carcinoma
Summary
Murine double minute 2 (MDM2) is involved in cell growth and differentiation through its interaction with other cellular proteins (Uldrijan et al, 2007; Wang et al, 2009). MDM2 belongs to the family of RING Finger ubiquitin ligases (Jackson et al, 2000; Huang and Tindall, 2011), and the principal function of MDM2 is to mediate the ubiquitination and proteasome-dependent degradation of the p53 tumor suppressor protein and other growth regulatory proteins (Grossman et al, 1998; Manfredi, 2010; Chansaenroj et al, 2013). SCY1-like 1-binding protein 1 (SCYL1BP1) is a newly identified regulator of Mdm, which directly binds to Mdm and promotes Mdm self-ubiquitination, subsequently stabilizing p53 (Yan et al, 2010a; Yan et al, 2010b). The interaction between SCYL1BP1 and MDM2 in human lung squamous carcinoma remained unknown, and the effects of SCYL1BP1 on lung squamous carcinoma cell biological behaviors still remains poorly understood
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