INVESTIGADORES
MOLEJON Maria Ines
capítulos de libros
Título:
Beclin 1
Autor/es:
MOLEJON MI; ROPOLO A; VACCARO, MI
Libro:
The Pancreapedia - The Exocrine Pancreas: Current Concepts of Health and Disease
Editorial:
Michigan Publishing
Referencias:
Año: 2012; p. 1 - 9
Resumen:
Beclin 1/ATG6/Vps30 (UniProtKB/Swiss-Prot Q14457) is a 450 amino-acids length protein, with three domains; BH3 (aminoacid 114 to 123), Coiled Coil domain (CCD; aminoacid 144 to 269) and the Evolutionarily Conserved Domain (ECD; aminoacid 244 to 337). BH3 proteins are part of the Bcl-2 family; they are pro-apoptotic damage sensors that play an important role in protecting against cancer. The BH3-only domain of Beclin 1 can interact with Bcl-2 and Bcl-XL. Both cellular and viral Bcl-2 (vBcl-2), or more specifically ER-targeted Bcl-2, inhibit Beclin 1-dependent autophagy by interfering with the Beclin 1-PtdIns 3-kinase interaction (PI3K) and the Beclin 1-associated PI3K activity. The interaction between Bcl-2 and Beclin 1 is greatly reduced upon starvation, which suggests that the dissociation of Bcl-2 from Beclin1 is important for activating autophagy. We demonstrated that, VMP1 (Vacuole Membrane Protein 1) displaces Bcl-2 from Beclin 1, partitioning Beclin 1 to the autophagic pathway.