Difference between revisions of "Phosphatase Subfamily CDC14"

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=== Evolution ===
 
=== Evolution ===
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CDC14 is found in most eukaryotes with the exception of higher plants. Most vertebrates express two paralogs typically designated CDC14A and CDC14B (see [http://resdev.gene.com/gOrtholog/view/cluster/MC0000760/overview unpublished data from gOrtholog]).  
 
CDC14 is found in most eukaryotes with the exception of higher plants. Most vertebrates express two paralogs typically designated CDC14A and CDC14B (see [http://resdev.gene.com/gOrtholog/view/cluster/MC0000760/overview unpublished data from gOrtholog]).  
  
 
=== Domain ===
 
=== Domain ===
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+
CDC14 has two tandem structural equivalent domains linked by an alpha helix. Both domains have a DSP fold and the second domain is catalytic active. CDC14 also has a conserved nuclear export sequence (NES) at C-terminal; human CDC14s has nucleolar targeting sequence at N-terminal <cite>Gray03</cite>.
CDC14 has a conserved domain combination: N-terminal phosphatase domain and nuclear export sequence (NES) <cite>Mocciaro10</cite>.
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=== Function ===
 
=== Function ===
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Unlike the budding yeast enzyme, Cdc14 orthologs of most other species are not required for mitotic exit <cite>Mocciaro10, Bremmer12</cite>. In vertebrates, there are conflicting reports on the functions of the Cdc14 isoforms, but there is evidence for involvement in regulating mitotic entry, centrosome duplication, DNA repair, and cytokinesis <cite>Mocciaro10, Bremmer12</cite>.  
 
Unlike the budding yeast enzyme, Cdc14 orthologs of most other species are not required for mitotic exit <cite>Mocciaro10, Bremmer12</cite>. In vertebrates, there are conflicting reports on the functions of the Cdc14 isoforms, but there is evidence for involvement in regulating mitotic entry, centrosome duplication, DNA repair, and cytokinesis <cite>Mocciaro10, Bremmer12</cite>.  
  
 
=== References ===
 
=== References ===
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<biblio>
 
<biblio>
 
#Bremmer12 pmid=22117071
 
#Bremmer12 pmid=22117071
 +
#Gray03 pmid=12853468
 
#Mocciaro10 pmid=20720150
 
#Mocciaro10 pmid=20720150
 
</biblio>
 
</biblio>

Revision as of 17:08, 5 May 2015

Phosphatase Classification: Fold CC1: Superfamily CC1: Family DSP: Subfamily CDC14

CDC14 subfamily consists of cell cycle genes widely found in eukaryotes with the exception of higher plants.

Evolution

CDC14 is found in most eukaryotes with the exception of higher plants. Most vertebrates express two paralogs typically designated CDC14A and CDC14B (see unpublished data from gOrtholog).

Domain

CDC14 has two tandem structural equivalent domains linked by an alpha helix. Both domains have a DSP fold and the second domain is catalytic active. CDC14 also has a conserved nuclear export sequence (NES) at C-terminal; human CDC14s has nucleolar targeting sequence at N-terminal [1].

Function

Unlike the budding yeast enzyme, Cdc14 orthologs of most other species are not required for mitotic exit [2, 3]. In vertebrates, there are conflicting reports on the functions of the Cdc14 isoforms, but there is evidence for involvement in regulating mitotic entry, centrosome duplication, DNA repair, and cytokinesis [2, 3].

References

  1. Gray CH, Good VM, Tonks NK, and Barford D. The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase. EMBO J. 2003 Jul 15;22(14):3524-35. DOI:10.1093/emboj/cdg348 | PubMed ID:12853468 | HubMed [Gray03]
  2. Mocciaro A and Schiebel E. Cdc14: a highly conserved family of phosphatases with non-conserved functions?. J Cell Sci. 2010 Sep 1;123(Pt 17):2867-76. DOI:10.1242/jcs.074815 | PubMed ID:20720150 | HubMed [Mocciaro10]
  3. Bremmer SC, Hall H, Martinez JS, Eissler CL, Hinrichsen TH, Rossie S, Parker LL, Hall MC, and Charbonneau H. Cdc14 phosphatases preferentially dephosphorylate a subset of cyclin-dependent kinase (Cdk) sites containing phosphoserine. J Biol Chem. 2012 Jan 13;287(3):1662-9. DOI:10.1074/jbc.M111.281105 | PubMed ID:22117071 | HubMed [Bremmer12]
All Medline abstracts: PubMed | HubMed