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J Biol Chem, Vol. 274, Issue 3, 1533-1540, January 15, 1999
From the 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.
Cloning of AIP1, a Novel Protein That Associates with the
Apoptosis-linked Gene ALG-2 in a Ca2+-dependent
Reaction
§,,
T-cell Molecular Biology Unit,
Laboratory of Cellular and Molecular Immunology, NIAID, National
Institutes of Health, Bethesda, Maryland 20892 and the
§ Basel Institute for Immunology, Grenzacherstrasse 487, Postfach CH-4005, Basel, Switzerland
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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 C. Thery, M. Boussac, P. Veron, P. Ricciardi-Castagnoli, G. Raposo, J. Garin, and S. Amigorena Proteomic Analysis of Dendritic Cell-Derived Exosomes: A Secreted Subcellular Compartment Distinct from Apoptotic Vesicles J. Immunol., June 15, 2001; 166(12): 7309 - 7318. [Abstract] [Full Text] [PDF]
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S. Tarabykina, A. L. Moller, I. Durussel, J. Cox, and M. W. Berchtold Two Forms of the Apoptosis-linked Protein ALG-2 with Different Ca2+ Affinities and Target Recognition J. Biol. Chem., March 31, 2000; 275(14): 10514 - 10518. [Abstract] [Full Text] [PDF]
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B. J. Passer, L. Pellegrini, P. Vito, J. K. Ganjei, and L. D'Adamio Interaction of Alzheimer's Presenilin-1 and Presenilin-2 with Bcl-XL. A POTENTIAL ROLE IN MODULATING THE THRESHOLD OF CELL DEATH J. Biol. Chem., August 20, 1999; 274(34): 24007 - 24013. [Abstract] [Full Text] [PDF]
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Y. Kitaura, S. Matsumoto, H. Satoh, K. Hitomi, and M. Maki Peflin and ALG-2, Members of the Penta-EF-Hand Protein Family, Form a Heterodimer That Dissociates in a Ca2+-dependent Manner J. Biol. Chem., April 20, 2001; 276(17): 14053 - 14058. [Abstract] [Full Text] [PDF]
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M. H. Scheinfeld, R. Roncarati, P. Vito, P. A. Lopez, M. Abdallah, and L. D'Adamio Jun NH2-terminal Kinase (JNK) Interacting Protein 1 (JIP1) Binds the Cytoplasmic Domain of the Alzheimer's beta -Amyloid Precursor Protein (APP) J. Biol. Chem., January 25, 2002; 277(5): 3767 - 3775. [Abstract] [Full Text] [PDF]
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B. Chen, S. C. Borinstein, J. Gillis, V. W. Sykes, and O. Bogler The Glioma-associated Protein SETA Interacts with AIP1/Alix and ALG-2 and Modulates Apoptosis in Astrocytes J. Biol. Chem., June 16, 2000; 275(25): 19275 - 19281. [Abstract] [Full Text] [PDF]
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