Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis

Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis

2007 October : 9(10): 1142–1151 | Yoshinori Takahashi, Domenico Coppola, Norimasa Matsushita, Hernani D. Cualing, Mei Sun, Yuya Sato, Chengyu Liang, Jae U. Jung, Jin Q. Cheng, James J. Mulé, W. Jack Pledger, and Hong-Gang Wang
This study investigates the role of Bif-1 (Endophillin B1) in autophagy and tumorigenesis. Bif-1 interacts with Beclin 1 through UVRAG and acts as a positive regulator of the class III PI3-kinase (PI3KC3). In response to nutrient deprivation, Bif-1 localizes to autophagosomes, where it colocalizes with Atg5 and LC3. Loss of Bif-1 suppresses autophagosome formation and cell death, suggesting that Bif-1 is essential for autophagy-dependent cell survival. Furthermore, Bif-1 ablation prolongs cell survival under nutrient starvation and significantly enhances spontaneous tumor development in mice. These findings indicate that Bif-1 joins the UVRAG-Beclin 1 complex as a potential activator of autophagy and tumor suppressor.This study investigates the role of Bif-1 (Endophillin B1) in autophagy and tumorigenesis. Bif-1 interacts with Beclin 1 through UVRAG and acts as a positive regulator of the class III PI3-kinase (PI3KC3). In response to nutrient deprivation, Bif-1 localizes to autophagosomes, where it colocalizes with Atg5 and LC3. Loss of Bif-1 suppresses autophagosome formation and cell death, suggesting that Bif-1 is essential for autophagy-dependent cell survival. Furthermore, Bif-1 ablation prolongs cell survival under nutrient starvation and significantly enhances spontaneous tumor development in mice. These findings indicate that Bif-1 joins the UVRAG-Beclin 1 complex as a potential activator of autophagy and tumor suppressor.
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Understanding Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis