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.
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
J. Biol. Chem.
Date: Jan. 15, 1999
Download Curated Data For This Publication
10086
Switch View:
  • Interactions 3