FHA-RING ubiquitin ligases in cell division cycle control |
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Authors: | L. Brooks III E. G. Heimsath Jr. G. L. Loring C. Brenner |
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Affiliation: | (1) Departments of Genetics and Biochemistry and Norris Cotton Cancer Center, Dartmouth Medical School, Rubin 733–HB7937, Lebanon, NH 03756, USA;(2) Altus Pharmaceuticals, Cambridge, MA 02139, USA |
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Abstract: | Despite the common occurrence of forkhead associated (FHA) phosphopeptide-binding domains and really interesting new gene (RING) E3 ubiquitin ligase domains, gene products containing both an N-terminal FHA domain and C-terminal RING domain constitute a highly distinctive intersection. Characterized FHA-RING ligases include the two vertebrate proteins, Checkpoint with FHA and RING (Chfr) and RING finger 8 (Rnf8), as well as three fungal proteins, Defective in mitosis (Dma1), Chf1 and Chf2. These FHA-RING ligases play roles in negative regulation of the cell division cycle, apparently by coupling protein phosphorylation events to specific ubiquitylation of target proteins. Here, the available data on upstream and downstream regulation of and by FHA-RING ligases are reviewed. Received 24 April 2008; received after revision 18 June 2008; accepted 20 June 2008 |
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Keywords: | KeywordHeading" >. Cell cycle checkpoint E3 ubiquitin ligase Ubc4 Ubc13/Mms2 |
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