Functions of BCL-XL at the Interface between Cell Death and Metabolism
The BCL-2 homolog BCL-XL, one of the two protein products of BCL2L1, has originally been characterized for its prominent prosurvival functions. Similar to BCL-2, BCL-XL binds to its multidomain proapoptotic counterparts BAX and BAK, hence preventing the formation of lethal pores in the mitochondrial...
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| Format: | Article |
| Language: | English |
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Wiley
2013-01-01
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| Series: | International Journal of Cell Biology |
| Online Access: | http://dx.doi.org/10.1155/2013/705294 |
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| author | Judith Michels Oliver Kepp Laura Senovilla Delphine Lissa Maria Castedo Guido Kroemer Lorenzo Galluzzi |
| author_facet | Judith Michels Oliver Kepp Laura Senovilla Delphine Lissa Maria Castedo Guido Kroemer Lorenzo Galluzzi |
| author_sort | Judith Michels |
| collection | DOAJ |
| description | The BCL-2 homolog BCL-XL, one of the two protein products of BCL2L1, has originally been characterized for its prominent prosurvival functions. Similar to BCL-2, BCL-XL binds to its multidomain proapoptotic counterparts BAX and BAK, hence preventing the formation of lethal pores in the mitochondrial outer membrane, as well as to multiple BH3-only proteins, thus interrupting apical proapoptotic signals. In addition, BCL-XL has been suggested to exert cytoprotective functions by sequestering a cytosolic pool of the pro-apoptotic transcription factor p53 and by binding to the voltage-dependent anion channel 1 (VDAC1), thereby inhibiting the so-called mitochondrial permeability transition (MPT). Thus, BCL-XL appears to play a prominent role in the regulation of multiple distinct types of cell death, including apoptosis and regulated necrosis. More recently, great attention has been given to the cell death-unrelated functions of BCL-2-like proteins. In particular, BCL-XL has been shown to modulate a number of pathophysiological processes, including—but not limited to—mitochondrial ATP synthesis, protein acetylation, autophagy and mitosis. In this short review article, we will discuss the functions of BCL-XL at the interface between cell death and metabolism. |
| format | Article |
| id | doaj-art-609dbcda000444098fe3a76db53b5e09 |
| institution | Kabale University |
| issn | 1687-8876 1687-8884 |
| language | English |
| publishDate | 2013-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | International Journal of Cell Biology |
| spelling | doaj-art-609dbcda000444098fe3a76db53b5e092025-02-03T01:25:31ZengWileyInternational Journal of Cell Biology1687-88761687-88842013-01-01201310.1155/2013/705294705294Functions of BCL-XL at the Interface between Cell Death and MetabolismJudith Michels0Oliver Kepp1Laura Senovilla2Delphine Lissa3Maria Castedo4Guido Kroemer5Lorenzo Galluzzi6INSERM, U848, Institut Gustave Roussy, Pavillon de Recherche 1, 39 Rue Camille Desmoulins, 94805 Villejuif, FranceINSERM, U848, Institut Gustave Roussy, Pavillon de Recherche 1, 39 Rue Camille Desmoulins, 94805 Villejuif, FranceINSERM, U848, Institut Gustave Roussy, Pavillon de Recherche 1, 39 Rue Camille Desmoulins, 94805 Villejuif, FranceINSERM, U848, Institut Gustave Roussy, Pavillon de Recherche 1, 39 Rue Camille Desmoulins, 94805 Villejuif, FranceINSERM, U848, Institut Gustave Roussy, Pavillon de Recherche 1, 39 Rue Camille Desmoulins, 94805 Villejuif, FranceINSERM, U848, Institut Gustave Roussy, Pavillon de Recherche 1, 39 Rue Camille Desmoulins, 94805 Villejuif, FranceInstitut Gustave Roussy, 94805 Villejuif, FranceThe BCL-2 homolog BCL-XL, one of the two protein products of BCL2L1, has originally been characterized for its prominent prosurvival functions. Similar to BCL-2, BCL-XL binds to its multidomain proapoptotic counterparts BAX and BAK, hence preventing the formation of lethal pores in the mitochondrial outer membrane, as well as to multiple BH3-only proteins, thus interrupting apical proapoptotic signals. In addition, BCL-XL has been suggested to exert cytoprotective functions by sequestering a cytosolic pool of the pro-apoptotic transcription factor p53 and by binding to the voltage-dependent anion channel 1 (VDAC1), thereby inhibiting the so-called mitochondrial permeability transition (MPT). Thus, BCL-XL appears to play a prominent role in the regulation of multiple distinct types of cell death, including apoptosis and regulated necrosis. More recently, great attention has been given to the cell death-unrelated functions of BCL-2-like proteins. In particular, BCL-XL has been shown to modulate a number of pathophysiological processes, including—but not limited to—mitochondrial ATP synthesis, protein acetylation, autophagy and mitosis. In this short review article, we will discuss the functions of BCL-XL at the interface between cell death and metabolism.http://dx.doi.org/10.1155/2013/705294 |
| spellingShingle | Judith Michels Oliver Kepp Laura Senovilla Delphine Lissa Maria Castedo Guido Kroemer Lorenzo Galluzzi Functions of BCL-XL at the Interface between Cell Death and Metabolism International Journal of Cell Biology |
| title | Functions of BCL-XL at the Interface between Cell Death and Metabolism |
| title_full | Functions of BCL-XL at the Interface between Cell Death and Metabolism |
| title_fullStr | Functions of BCL-XL at the Interface between Cell Death and Metabolism |
| title_full_unstemmed | Functions of BCL-XL at the Interface between Cell Death and Metabolism |
| title_short | Functions of BCL-XL at the Interface between Cell Death and Metabolism |
| title_sort | functions of bcl xl at the interface between cell death and metabolism |
| url | http://dx.doi.org/10.1155/2013/705294 |
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