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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2007-10

AUTHORS

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, Hong-Gang Wang

ABSTRACT

Autophagy is an evolutionarily conserved 'self-eating' process. Although the genes essential for autophagy (named Atg) have been identified in yeast, the molecular mechanism of how Atg proteins control autophagosome formation in mammalian cells remains to be elucidated. Here, we demonstrate that Bif-1 (also known as Endophilin B1) interacts with Beclin 1 through ultraviolet irradiation resistance-associated gene (UVRAG) and functions as a positive mediator of the class III PI(3) kinase (PI(3)KC3). In response to nutrient deprivation, Bif-1 localizes to autophagosomes where it colocalizes with Atg5, as well as microtubule-associated protein light chain 3 (LC3). Furthermore, loss of Bif-1 suppresses autophagosome formation. Although the SH3 domain of Bif-1 is sufficient for binding to UVRAG, both the BAR and SH3 domains are required for Bif-1 to activate PI(3)KC3 and induce autophagosome formation. We also observed that Bif-1 ablation prolongs cell survival under starvation conditions. Moreover, knockout of Bif-1 significantly enhances the development of spontaneous tumours in mice. These findings suggest that Bif-1 joins the UVRAG-Beclin 1 complex as a potential activator of autophagy and tumour suppressor. More... »

PAGES

1142-1151

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncb1634

DOI

http://dx.doi.org/10.1038/ncb1634

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1004639306

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17891140


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