Regulation of the Fanconi anemia group C protein through proteolytic modification
| Autor: | Chantal Godin, Caroline C. Huard, Cedric S. Tremblay, Manuel Buchwald, Isabelle Brodeur, Isabelle Goulet, Edward W. Khandjian, Georges Lévesque, Madeleine Carreau, Marie Chantal Delisle, Chantal Charbonneau |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
congenital
hereditary and neonatal diseases and abnormalities Fanconi anemia complementation group C Mitomycin Apoptosis Cell Cycle Proteins Transfection Biochemistry Cell Line GSTP1 Ubiquitin Fanconi anemia hemic and lymphatic diseases medicine Humans Nuclear protein Molecular Biology Caspase Sequence Deletion Binding Sites biology Effector Fanconi Anemia Complementation Group C Protein nutritional and metabolic diseases Nuclear Proteins Proteins Cell Biology medicine.disease Molecular biology Fanconi Anemia Complementation Group Proteins Peptide Fragments Recombinant Proteins DNA-Binding Proteins Molecular Weight Fanconi Anemia Caspases biology.protein Mutagenesis Site-Directed Protein Processing Post-Translational HeLa Cells |
| Zdroj: | The Journal of biological chemistry. 279(6) |
| ISSN: | 0021-9258 |
| Popis: | The function of the Fanconi anemia group C protein (FANCC) is still unknown, though many studies point to a role in damage response signaling. Unlike other known FA proteins, FANCC is mainly localized to the cytoplasm and is thought to act as a messenger of cellular damage rather than an effector of repair. FANCC has been shown to interact with several cytoplasmic and nuclear proteins and to delay the onset of apoptosis through redox regulation of GSTP1. We investigated the fate and function of FANCC during apoptosis. Here we show that FANCC undergoes proteolytic modification by a caspase into a predominant 47-kDa ubiquitinated protein fragment. Lack of proteolytic modification at the putative cleavage site delays apoptosis but does not affect MMC complementation. These results suggest that FANCC function is regulated through proteolytic processing. |
| Databáze: | OpenAIRE |
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