Abstract
Members of the caspase family are essential executors of apoptosis. Caspase-2 has two messenger RNAs generated by alternative splicing, which encode caspase-2L and caspase-2S. Although caspase-2L induces apoptosis, caspase-2S also has the ability to antagonize cell death. Experiments in caspase-2-deficient mice showed that caspase-2 functions to delay cell death in some neuronal populations, suggesting that caspase-2S dominantly acts for cell survival in the brain. However, the mechanism of caspase-2S-mediated anti-apoptotic effect is still unclear. Here, we isolated a protein that interacts with caspase-2S, designated as Ich-1S (caspase-2S)-binding protein (ISBP), by yeast two-hybrid screening using full-length caspase-2S cDNA as a bait. ISBP is identical to the recently isolated calcium and integrin-binding protein, and a small molecule calcium-binding protein with two EF-hand motifs of its C-terminus. In vitro transcribed and translated ISBP interacts specifically with glutathione-S-transferase-fused caspase-2S. Moreover, the interaction between ISBP and caspase-2S was observed in cultured cells. Northern blot analysis indicated that ISBP may be a ubiquitous protein. Interestingly, ISBP can partially inhibit the processing of pro-caspase-2L induced by anti-Fas antibody-treated Jurkat cytosolic lysates. These results suggested that ISBP may be the mediator for the survival function of caspase-2S. Copyright (C) 2000 Federation of European Biochemical Societies.
| Original language | English |
|---|---|
| Pages (from-to) | 360-364 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 470 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Mar 31 2000 |
| Externally published | Yes |
Fingerprint
Keywords
- Apoptosis
- Caspase-2
- Caspase-2S
- Ich-1S-binding protein
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Isolation of Ich-1S (caspase-2S)-binding protein that partially inhibits caspase activity. / Ito, Akihiro; Uehara, Takashi; Nomura, Yasuyuki.
In: FEBS Letters, Vol. 470, No. 3, 31.03.2000, p. 360-364.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Isolation of Ich-1S (caspase-2S)-binding protein that partially inhibits caspase activity
AU - Ito, Akihiro
AU - Uehara, Takashi
AU - Nomura, Yasuyuki
PY - 2000/3/31
Y1 - 2000/3/31
N2 - Members of the caspase family are essential executors of apoptosis. Caspase-2 has two messenger RNAs generated by alternative splicing, which encode caspase-2L and caspase-2S. Although caspase-2L induces apoptosis, caspase-2S also has the ability to antagonize cell death. Experiments in caspase-2-deficient mice showed that caspase-2 functions to delay cell death in some neuronal populations, suggesting that caspase-2S dominantly acts for cell survival in the brain. However, the mechanism of caspase-2S-mediated anti-apoptotic effect is still unclear. Here, we isolated a protein that interacts with caspase-2S, designated as Ich-1S (caspase-2S)-binding protein (ISBP), by yeast two-hybrid screening using full-length caspase-2S cDNA as a bait. ISBP is identical to the recently isolated calcium and integrin-binding protein, and a small molecule calcium-binding protein with two EF-hand motifs of its C-terminus. In vitro transcribed and translated ISBP interacts specifically with glutathione-S-transferase-fused caspase-2S. Moreover, the interaction between ISBP and caspase-2S was observed in cultured cells. Northern blot analysis indicated that ISBP may be a ubiquitous protein. Interestingly, ISBP can partially inhibit the processing of pro-caspase-2L induced by anti-Fas antibody-treated Jurkat cytosolic lysates. These results suggested that ISBP may be the mediator for the survival function of caspase-2S. Copyright (C) 2000 Federation of European Biochemical Societies.
AB - Members of the caspase family are essential executors of apoptosis. Caspase-2 has two messenger RNAs generated by alternative splicing, which encode caspase-2L and caspase-2S. Although caspase-2L induces apoptosis, caspase-2S also has the ability to antagonize cell death. Experiments in caspase-2-deficient mice showed that caspase-2 functions to delay cell death in some neuronal populations, suggesting that caspase-2S dominantly acts for cell survival in the brain. However, the mechanism of caspase-2S-mediated anti-apoptotic effect is still unclear. Here, we isolated a protein that interacts with caspase-2S, designated as Ich-1S (caspase-2S)-binding protein (ISBP), by yeast two-hybrid screening using full-length caspase-2S cDNA as a bait. ISBP is identical to the recently isolated calcium and integrin-binding protein, and a small molecule calcium-binding protein with two EF-hand motifs of its C-terminus. In vitro transcribed and translated ISBP interacts specifically with glutathione-S-transferase-fused caspase-2S. Moreover, the interaction between ISBP and caspase-2S was observed in cultured cells. Northern blot analysis indicated that ISBP may be a ubiquitous protein. Interestingly, ISBP can partially inhibit the processing of pro-caspase-2L induced by anti-Fas antibody-treated Jurkat cytosolic lysates. These results suggested that ISBP may be the mediator for the survival function of caspase-2S. Copyright (C) 2000 Federation of European Biochemical Societies.
KW - Apoptosis
KW - Caspase-2
KW - Caspase-2S
KW - Ich-1S-binding protein
UR - http://www.scopus.com/inward/record.url?scp=0034737397&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034737397&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(00)01351-X
DO - 10.1016/S0014-5793(00)01351-X
M3 - Article
C2 - 10745097
AN - SCOPUS:0034737397
VL - 470
SP - 360
EP - 364
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 3
ER -