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

Pasquale Vito, Luca Pellegrini, Chantal Guiet, Luciano D'Adamio

Research output: Contribution to journalArticle

197 Scopus citations

Abstract

ALG-2 is a 22-kDa calcium-binding protein necessary for cell death induced by different stimuli in 3DO T-cell hyhridoma. 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.

Original languageEnglish (US)
Pages (from-to)1533-1540
Number of pages8
JournalJournal of Biological Chemistry
Volume274
Issue number3
DOIs
StatePublished - Jan 15 1999

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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