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Cited by 254

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Phosphorylation of Beclin 1 by DAP-kinase promotes autophagy by weakening its interactions with Bcl-2 and Bcl-XL

Open access
Zalckvar, Einat, Berissi, Hanna, Eisenstein, Miriam, Kimchi, Adi·2009·Autophagy

Abstract

Beclin 1, an essential autophagic protein, is a BH3-only protein that binds Bcl-2 anti-apoptotic family members. The dissociation of Beclin 1 from the Bcl-2 inhibitors is essential for its autophagic activity, and therefore is tightly controlled. We recently revealed a novel phosphorylation-based mechanism by which death-associated protein kinase (DAPk) regulates this process. We found that DAPk phosphorylates Beclin 1 on T119, a critical residue within its BH3 domain, and thus promotes Beclin 1 dissociation from Bcl-X(L) and autophagy induction. Here we report that T119 phosphorylation also reduces the interaction between Beclin 1 and Bcl-2, in line with the high degree of structural homology between the BH3 binding pockets of Bcl-2 and Bcl-X(L) proteins. Our results reveal a new phosphorylation-based mechanism that reduces the interaction of Beclin 1 with its inhibitors to activate the autophagic machinery.

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Metadata

Authors
Zalckvar, E., Berissi, H., Eisenstein, M., & Kimchi, A.
Venue
Autophagy
Published
2009-07
Volume
5
Issue
5
Pages
720-722
ISSN
  • 1554-8627 (ISSN-L)
  • 1554-8635
OpenAlex
W1994411647
Cited by
254
References
3
FWCI
10.28
Type
journal article
Language
en
Open access
bronze

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