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Cloning of AIP1, a novel protein that associates with the apoptosis-linked gene ALG-2 in a Ca2+-dependent reaction.

ALG-2 is a 22-kDa calcium-binding protein necessary for cell death induced by different stimuli in 3DO T-cell hybridoma. 3DO cell clones depleted of ALG-2 protein exhibit normal caspases activation, suggesting that ALG-2 function is required downstream or is independent of caspase proteases activity for apoptosis to occur. Using the yeast two-hybrid screening system, we have isolated and characterized the mouse cDNA encoding for ALG-2 interacting protein 1 (AIP1), a novel protein that interacts with ALG-2. ALG-2 and AIP1 colocalize in the cytosol and the presence of calcium is an indispensable requisite for their association. Sequence alignment shows that AIP1 is highly similar to BRO1, a yeast protein related to components of the Pkc1p-MAP kinase cascade. Overexpression of a truncated form of AIP1 protects two different cell types from death induced by trophic factors withdrawal; thus, our data indicate that AIP1 cooperates with ALG-2 in executing the calcium-dependent requirements along the cell death pathway.

Pubmed ID: 9880530


  • Vito P
  • Pellegrini L
  • Guiet C
  • D'Adamio L


The Journal of biological chemistry

Publication Data

January 15, 1999

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis
  • Apoptosis Regulatory Proteins
  • Blotting, Northern
  • COS Cells
  • Calcium
  • Calcium-Binding Proteins
  • Carrier Proteins
  • Cell Cycle Proteins
  • Cloning, Molecular
  • Cytosol
  • DNA-Binding Proteins
  • Endosomal Sorting Complexes Required for Transport
  • Fungal Proteins
  • HeLa Cells
  • Humans
  • Mice
  • Molecular Sequence Data
  • Molecular Weight
  • Rabbits
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors