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A novel caspase-2 complex containing TRAF2 and RIP1

(2005) JOURNAL OF BIOLOGICAL CHEMISTRY. 280(8). p.6923-6932
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Abstract
The enzymatic activity of caspases is implicated in the execution of apoptosis and inflammation. Here we demonstrate a novel nonenzymatic function for caspase-2 other than its reported proteolytic role in apoptosis. Caspase-2, unlike caspase-3, -6, -7, -9, -11, -12, and -14, is a potent inducer of NF-kappaB and p38 MAPK activation in a TRAF2-mediated way. Caspase-2 interacts with TRAF1, TRAF2, and RIP1. Furthermore, we demonstrate that endogenous caspase-2 is recruited into a large and inducible protein complex, together with TRAF2 and RIP1. Structure-function analysis shows that NF-kappaB activation occurs independent of enzymatic activity of the protease and that the caspase recruitment domain of caspase-2 is sufficient for the activation of NF-kappaB and p38 MAPK. These results demonstrate the inducible assembly of a novel protein complex consisting of caspase-2, TRAF2, and RIP1 that activates NF-kappaB and p38 MAPK through the caspase recruitment domain of caspase-2 independently of its proteolytic activity.
Keywords
TUMOR-NECROSIS-FACTOR, NF-KAPPA-B, ZINC-FINGER PROTEIN, DOMAIN KINASE RIP, SIGNAL-TRANSDUCTION PATHWAY, CELL-DEATH, FACTOR RECEPTOR, INDUCED APOPTOSIS, MEDIATED APOPTOSIS, ENZYMATIC-ACTIVITY

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Citation

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Chicago
Lamkanfi, Mohamed, Kathleen D’Hondt, Lieselotte Vande Walle, Maria Van Gurp, Geertrui Denecker, Jill Demeulemeester, Michaël Kalai, Wim Declercq, Xavier Saelens, and Peter Vandenabeele. 2005. “A Novel Caspase-2 Complex Containing TRAF2 and RIP1.” Journal of Biological Chemistry 280 (8): 6923–6932.
APA
Lamkanfi, M., D’Hondt, K., Vande Walle, L., Van Gurp, M., Denecker, G., Demeulemeester, J., Kalai, M., et al. (2005). A novel caspase-2 complex containing TRAF2 and RIP1. JOURNAL OF BIOLOGICAL CHEMISTRY, 280(8), 6923–6932.
Vancouver
1.
Lamkanfi M, D’Hondt K, Vande Walle L, Van Gurp M, Denecker G, Demeulemeester J, et al. A novel caspase-2 complex containing TRAF2 and RIP1. JOURNAL OF BIOLOGICAL CHEMISTRY. 2005;280(8):6923–32.
MLA
Lamkanfi, Mohamed, Kathleen D’Hondt, Lieselotte Vande Walle, et al. “A Novel Caspase-2 Complex Containing TRAF2 and RIP1.” JOURNAL OF BIOLOGICAL CHEMISTRY 280.8 (2005): 6923–6932. Print.
@article{300573,
  abstract     = {The enzymatic activity of caspases is implicated in the execution of apoptosis and inflammation. Here we demonstrate a novel nonenzymatic function for caspase-2 other than its reported proteolytic role in apoptosis. Caspase-2, unlike caspase-3, -6, -7, -9, -11, -12, and -14, is a potent inducer of NF-kappaB and p38 MAPK activation in a TRAF2-mediated way. Caspase-2 interacts with TRAF1, TRAF2, and RIP1. Furthermore, we demonstrate that endogenous caspase-2 is recruited into a large and inducible protein complex, together with TRAF2 and RIP1. Structure-function analysis shows that NF-kappaB activation occurs independent of enzymatic activity of the protease and that the caspase recruitment domain of caspase-2 is sufficient for the activation of NF-kappaB and p38 MAPK. These results demonstrate the inducible assembly of a novel protein complex consisting of caspase-2, TRAF2, and RIP1 that activates NF-kappaB and p38 MAPK through the caspase recruitment domain of caspase-2 independently of its proteolytic activity.},
  author       = {Lamkanfi, Mohamed and D'Hondt, Kathleen and Vande Walle, Lieselotte and Van Gurp, Maria and Denecker, Geertrui and Demeulemeester, Jill and Kalai, Micha{\"e}l and Declercq, Wim and Saelens, Xavier and Vandenabeele, Peter},
  issn         = {0021-9258},
  journal      = {JOURNAL OF BIOLOGICAL CHEMISTRY},
  language     = {eng},
  number       = {8},
  pages        = {6923--6932},
  title        = {A novel caspase-2 complex containing TRAF2 and RIP1},
  url          = {http://dx.doi.org/10.1074/jbc.M411180200},
  volume       = {280},
  year         = {2005},
}

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