Difference between revisions of "Phosphatase Subfamily CDC25"
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=== Catalytic activity and functions === | === Catalytic activity and functions === | ||
| − | Cdc25 phosphatases, as activators of the Cdk/cyclins, play critical roles in the regulation of the eukaryotic cell cycle. Their structures and functions have been reviewed in | + | Cdc25 phosphatases, as activators of the Cdk/cyclins, play critical roles in the regulation of the eukaryotic cell cycle. Their structures and functions have been reviewed in detail <cite>boutros06, rudolph07, boutros07</cite>. |
=== References === | === References === | ||
Revision as of 17:38, 22 August 2015
Phosphatase Classification: Fold CC3 (Rhondanese): Superfamily CC3 (Rhondanese): Family CDC25: Subfamily CDC25
Evolution
CDC25 subfamily is found in a broad of eukaryotes, but absent from most if not all of plants. It has multiple copies in some if not many genomes. For example, human, fruit fly and C elegans have 3, 2, 4, respectively, and they do not fall into 1:1 orthologous relationship.
Domain
Human CDC25s have an N-terminal regulatory domain and phosphatase domain, called M-phase inducer phosphatase domain in Pfam. Due to alternative splicing, the isoforms of human CDC25s have different sequences at regulatory domain region. The N-terminal regulatory domain is found in most deuterostomes, but not protostomes.
Catalytic activity and functions
Cdc25 phosphatases, as activators of the Cdk/cyclins, play critical roles in the regulation of the eukaryotic cell cycle. Their structures and functions have been reviewed in detail [1, 2, 3].
References
- Boutros R, Dozier C, and Ducommun B. The when and wheres of CDC25 phosphatases. Curr Opin Cell Biol. 2006 Apr;18(2):185-91. DOI:10.1016/j.ceb.2006.02.003 |
- Rudolph J. Cdc25 phosphatases: structure, specificity, and mechanism. Biochemistry. 2007 Mar 27;46(12):3595-604. DOI:10.1021/bi700026j |
- Boutros R, Lobjois V, and Ducommun B. CDC25 phosphatases in cancer cells: key players? Good targets?. Nat Rev Cancer. 2007 Jul;7(7):495-507. DOI:10.1038/nrc2169 |
