Crosstalk between apoptosis and autophagy within the Beclin 1 interactome

Maria Chiara Maiuri, Alfredo Criollo, Guido Kroemer

    Research output: Contribution to journalShort surveypeer-review

    226 Citations (Scopus)

    Abstract

    Although the essential genes for autophagy (Atg) have been identified, the molecular mechanisms through which Atg proteins control 'self eating' in mammalian cells remain elusive. Beclin 1 (Bec1), the mammalian orthologue of yeast Atg6, is part of the class III phosphatidylinositol 3-kinase (PI3K) complex that induces autophagy. The first among an increasing number of Bec1-interacting proteins that has been identified is the anti-apoptotic protein Bcl-2. The dissociation of Bec1 from Bcl-2 is essential for its autophagic activity, and Bcl-2 only inhibits autophagy when it is present in the endoplasmic reticulum (ER). A paper in this issue of the EMBO Journal has identified a novel protein, NAF-1 (nutrient-deprivation autophagy factor-1), that binds Bcl-2 at the ER. NAF-1 is a component of the inositol-1,4,5 trisphosphate (IP3) receptor complex, which contributes to the interaction of Bcl-2 with Bec1 and is required for Bcl-2 to functionally antagonize Bec1-mediated autophagy. This work provides mechanistic insights into how autophagy-and apoptosis-regulatory molecules crosstalk at the ER.

    Original languageEnglish
    Pages (from-to)515-516
    Number of pages2
    JournalEMBO Journal
    Volume29
    Issue number3
    DOIs
    Publication statusPublished - 1 Feb 2010

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