The autophagy effector Beclin 1

A novel BH3-only protein

S. Sinha, B. Levine

Research output: Contribution to journalArticle

257 Citations (Scopus)

Abstract

BH3 domains were originally discovered in the context of apoptosis regulators and they mediate binding of proapoptotic Bcl-2 family members to antiapoptotic Bcl-2 family members. Yet, recent studies indicate that BH3 domains do not function uniquely in apoptosis regulation; they also function in the regulation of another critical pathway involved in cellular and tissue homeostasis called autophagy. Antiapoptotic Bcl-2 homologs downregulate autophagy through interactions with the essential autophagy effector and haploinsufficient tumor suppressor, Beclin 1. Beclin 1 contains a BH3 domain, similar to that of Bcl-2 proteins, which is necessary and sufficient for binding to antiapoptotic Bcl-2 homologs and required for Bcl-2-mediated inhibition of autophagy. This review will summarize the evidence that the BH3 domain of Beclin 1 serves as a key structural motif that enables Bcl-2 to function not only as an antiapoptotic protein, but also as an antiautophagy protein.

Original languageEnglish (US)
JournalOncogene
Volume27
Issue numberSUPPL. 1
DOIs
StatePublished - Dec 2008

Fingerprint

Autophagy
Proteins
Apoptosis
Critical Pathways
Homeostasis
Down-Regulation
Beclin-1
Neoplasms

Keywords

  • Apoptosis
  • Autophagy
  • Bcl-2
  • Beclin 1
  • BH3-only
  • Tumor suppressor

ASJC Scopus subject areas

  • Molecular Biology
  • Cancer Research
  • Genetics

Cite this

The autophagy effector Beclin 1 : A novel BH3-only protein. / Sinha, S.; Levine, B.

In: Oncogene, Vol. 27, No. SUPPL. 1, 12.2008.

Research output: Contribution to journalArticle

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