Related F-box proteins control cell death in caenorhabditis elegans and human lymphoma

Michael Chiorazzi; Lixin Rui; Yandan Yang; Michele Ceribelli; Nima Tishbi; Carine W. Maurer; Stella M. Ranuncolo; Hong Zhao; Weihong Xu; Wing Chung C. Chan; Elaine S. Jaffe; Randy D. Gascoyne; Elias Campo; Andreas Rosenwald; German Ott; Jan Delabie; Lisa M. Rimsza; Shai Shaham; Louis M. Staudt

doi:10.1073/pnas.1217271110

Related F-box proteins control cell death in caenorhabditis elegans and human lymphoma

Michael Chiorazzi, Lixin Rui, Yandan Yang, Michele Ceribelli, Nima Tishbi, Carine W. Maurer, Stella M. Ranuncolo, Hong Zhao, Weihong Xu, Wing Chung C. Chan, Elaine S. Jaffe, Randy D. Gascoyne, Elias Campo, Andreas Rosenwald, German Ott, Jan Delabie, Lisa M. Rimsza, Shai Shaham, Louis M. Staudt

Laboratory Medicine and Pathology

Research output: Contribution to journal › Article › peer-review

38 Scopus citations

Abstract

Cell death is a common metazoan cell fate, and its inactivation is central to human malignancy. In Caenorhabditis elegans, apoptotic cell death occurs via the activation of the caspase CED-3 following binding of the EGL-1/BH3-only protein to the antiapoptotic CED-9/ BCL2 protein. Here we report a major alternative mechanism for caspase activation in vivo involving the F-box protein DRE-1. DRE-1 functions in parallel to EGL-1, requires CED-9 for activity, and binds to CED-9, suggesting that DRE-1 promotes apoptosis by inactivating CED-9. FBXO10, a human protein related to DRE-1, binds BCL2 and promotes its degradation, thereby initiating cell death. Moreover, some human diffuse large B-cell lymphomas have inactivating mutations in FBXO10 or express FBXO10 at low levels. Our results suggest that DRE-1/FBXO10 is a conserved regulator of apoptosis.

Original language	English (US)
Pages (from-to)	3943-3948
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	110
Issue number	10
DOIs	https://doi.org/10.1073/pnas.1217271110
State	Published - Mar 5 2013

Keywords

Cancer
Ubiquitin

ASJC Scopus subject areas

General

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Chiorazzi, M., Rui, L., Yang, Y., Ceribelli, M., Tishbi, N., Maurer, C. W., Ranuncolo, S. M., Zhao, H., Xu, W., Chan, W. C. C., Jaffe, E. S., Gascoyne, R. D., Campo, E., Rosenwald, A., Ott, G., Delabie, J., Rimsza, L. M., Shaham, S., & Staudt, L. M. (2013). Related F-box proteins control cell death in caenorhabditis elegans and human lymphoma. Proceedings of the National Academy of Sciences of the United States of America, 110(10), 3943-3948. https://doi.org/10.1073/pnas.1217271110

Chiorazzi, M, Rui, L, Yang, Y, Ceribelli, M, Tishbi, N, Maurer, CW, Ranuncolo, SM, Zhao, H, Xu, W, Chan, WCC, Jaffe, ES, Gascoyne, RD, Campo, E, Rosenwald, A, Ott, G, Delabie, J, Rimsza, LM, Shaham, S & Staudt, LM 2013, 'Related F-box proteins control cell death in caenorhabditis elegans and human lymphoma', Proceedings of the National Academy of Sciences of the United States of America, vol. 110, no. 10, pp. 3943-3948. https://doi.org/10.1073/pnas.1217271110

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abstract = "Cell death is a common metazoan cell fate, and its inactivation is central to human malignancy. In Caenorhabditis elegans, apoptotic cell death occurs via the activation of the caspase CED-3 following binding of the EGL-1/BH3-only protein to the antiapoptotic CED-9/ BCL2 protein. Here we report a major alternative mechanism for caspase activation in vivo involving the F-box protein DRE-1. DRE-1 functions in parallel to EGL-1, requires CED-9 for activity, and binds to CED-9, suggesting that DRE-1 promotes apoptosis by inactivating CED-9. FBXO10, a human protein related to DRE-1, binds BCL2 and promotes its degradation, thereby initiating cell death. Moreover, some human diffuse large B-cell lymphomas have inactivating mutations in FBXO10 or express FBXO10 at low levels. Our results suggest that DRE-1/FBXO10 is a conserved regulator of apoptosis.",

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AU - Chiorazzi, Michael

AU - Rui, Lixin

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AU - Ceribelli, Michele

AU - Tishbi, Nima

AU - Maurer, Carine W.

AU - Ranuncolo, Stella M.

AU - Zhao, Hong

AU - Xu, Weihong

AU - Chan, Wing Chung C.

AU - Jaffe, Elaine S.

AU - Gascoyne, Randy D.

AU - Campo, Elias

AU - Rosenwald, Andreas

AU - Ott, German

AU - Delabie, Jan

AU - Rimsza, Lisa M.

AU - Shaham, Shai

AU - Staudt, Louis M.

PY - 2013/3/5

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N2 - Cell death is a common metazoan cell fate, and its inactivation is central to human malignancy. In Caenorhabditis elegans, apoptotic cell death occurs via the activation of the caspase CED-3 following binding of the EGL-1/BH3-only protein to the antiapoptotic CED-9/ BCL2 protein. Here we report a major alternative mechanism for caspase activation in vivo involving the F-box protein DRE-1. DRE-1 functions in parallel to EGL-1, requires CED-9 for activity, and binds to CED-9, suggesting that DRE-1 promotes apoptosis by inactivating CED-9. FBXO10, a human protein related to DRE-1, binds BCL2 and promotes its degradation, thereby initiating cell death. Moreover, some human diffuse large B-cell lymphomas have inactivating mutations in FBXO10 or express FBXO10 at low levels. Our results suggest that DRE-1/FBXO10 is a conserved regulator of apoptosis.

AB - Cell death is a common metazoan cell fate, and its inactivation is central to human malignancy. In Caenorhabditis elegans, apoptotic cell death occurs via the activation of the caspase CED-3 following binding of the EGL-1/BH3-only protein to the antiapoptotic CED-9/ BCL2 protein. Here we report a major alternative mechanism for caspase activation in vivo involving the F-box protein DRE-1. DRE-1 functions in parallel to EGL-1, requires CED-9 for activity, and binds to CED-9, suggesting that DRE-1 promotes apoptosis by inactivating CED-9. FBXO10, a human protein related to DRE-1, binds BCL2 and promotes its degradation, thereby initiating cell death. Moreover, some human diffuse large B-cell lymphomas have inactivating mutations in FBXO10 or express FBXO10 at low levels. Our results suggest that DRE-1/FBXO10 is a conserved regulator of apoptosis.

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Related F-box proteins control cell death in caenorhabditis elegans and human lymphoma

Abstract

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