A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions

EMBO J. 1995 Nov 15;14(22):5589-96.

Abstract

Regulation of the cell death program involves physical interactions between different members of the Bcl-2 family that either promote or suppress apoptosis. The Bcl-2 homolog, Bak, promotes apoptosis and binds anti-apoptotic family members including Bcl-2 and Bcl-xL. We have identified a domain in Bak that is both necessary and sufficient for cytotoxic activity and binding to Bcl-xL. Sequences similar to this domain were identified in Bax and Bip1, two other proteins that promote apoptosis and interact with Bcl-xL, and were likewise critical for their capacity to kill cells and bind Bcl-xL. Thus, the domain is of central importance in mediating the function of multiple cell death-regulatory proteins that interact with Bcl-2 family members.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis Regulatory Proteins
  • Apoptosis*
  • Binding Sites
  • Cell Line
  • Conserved Sequence*
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Mitochondrial Proteins
  • Molecular Sequence Data
  • Protein Binding
  • Proteins / chemistry
  • Proto-Oncogene Proteins / chemistry
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-bcl-2
  • Sequence Homology, Amino Acid
  • bcl-2 Homologous Antagonist-Killer Protein
  • bcl-2-Associated X Protein
  • bcl-X Protein

Substances

  • Apoptosis Regulatory Proteins
  • BIK protein, human
  • Membrane Proteins
  • Mitochondrial Proteins
  • Proteins
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • bcl-2 Homologous Antagonist-Killer Protein
  • bcl-2-Associated X Protein
  • bcl-X Protein

Associated data

  • GENBANK/U34584