Regulation of Bcl-xl channel activity by calcium

J Biol Chem. 1998 Jul 10;273(28):17307-10. doi: 10.1074/jbc.273.28.17307.

Abstract

Recent studies have demonstrated that the anti-apoptotic proteins, Bcl-2 and Bcl-xl, with the carboxyl-terminal hydrophobic domain removed, form cation-selective channels in the lipid bilayer reconstitution system. However, the regulatory properties of these channels are unknown. In this study, we investigated the ion-conducting properties of full-length Bcl-xl in the lipid bilayer reconstitution system. Our findings indicate that Bcl-xl forms a cation-selective channel that conducts sodium but not calcium and that Bcl-xl channel activity is reversibly inhibited by luminal calcium with a half-dissociation constant of approximately 60 microM. This calcium-dependent regulation of the Bcl-xl channel provides new insights into the roles of calcium and Bcl-2-related proteins in the programmed cell death pathway.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Apoptosis*
  • Base Sequence
  • Calcium / metabolism*
  • DNA Primers
  • Humans
  • Ion Channels / antagonists & inhibitors
  • Ion Channels / metabolism*
  • Proto-Oncogene Proteins c-bcl-2 / antagonists & inhibitors
  • Proto-Oncogene Proteins c-bcl-2 / metabolism*
  • bcl-X Protein

Substances

  • BCL2L1 protein, human
  • DNA Primers
  • Ion Channels
  • Proto-Oncogene Proteins c-bcl-2
  • bcl-X Protein
  • Calcium