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Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity.

Using a protein interaction cloning technique, we identified cDNAs that encode a novel Bcl-2-binding protein, termed BAG-1. The BAG-1 protein shares no significant homology with Bcl-2 or other Bcl-2 family proteins, which can form homo- and heterodimers. In gene transfer experiments using a human lymphoid cell line, Jurkat, coexpression of BAG-1 and Bcl-2 provided markedly increased protection from cell death induced by several stimuli, including staurosporine, anti-Fas antibody, and cytolytic T cells, relative to cells that contained gene transfer-mediated elevations in either BAG-1 or Bcl-2 protein alone. BAG-transfected 3T3 fibroblasts also exhibited prolonged cell survival in response to an apoptotic stimulus. The findings indicate that bag-1 represents a new type of anti-cell death gene and suggest that some routes of apoptosis induction previously ascribed to Bcl-2-independent pathways may instead reflect a need for the combination of Bcl-2 and BAG-1.

Pubmed ID: 7834747

Authors

  • Takayama S
  • Sato T
  • Krajewski S
  • Kochel K
  • Irie S
  • Millan JA
  • Reed JC

Journal

Cell

Publication Data

January 27, 1995

Associated Grants

  • Agency: NCI NIH HHS, Id: CA-60181

Mesh Terms

  • 3T3 Cells
  • Alkaloids
  • Amino Acid Sequence
  • Animals
  • Carrier Proteins
  • Cell Death
  • Cell Line
  • Cell Survival
  • Cloning, Molecular
  • DNA-Binding Proteins
  • Gene Library
  • Humans
  • Kinetics
  • Mice
  • Molecular Sequence Data
  • Protein Binding
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Radiation-Sensitizing Agents
  • Recombinant Fusion Proteins
  • Staurosporine
  • Substrate Specificity
  • Transcription Factors
  • Transfection
  • Tumor Cells, Cultured