Phosphatase Subfamily CDC14 - Revision history

Gerard: /* Function */

2017-04-01T19:33:53Z

‎Function

Gerard: /* Domain Architecture */

2017-04-01T19:33:10Z

‎Domain Architecture

Gerard: /* Function */

2016-09-10T13:56:46Z

‎Function

Gerard at 06:18, 4 February 2016

2016-02-04T06:18:20Z

Mark: /* References */

2015-09-15T20:01:30Z

‎References

Mark: /* Function */

2015-09-15T20:01:16Z

‎Function

Mark: /* Domain */

2015-06-29T17:14:20Z

‎Domain

Mark: /* References */

2015-06-20T14:40:08Z

‎References

Mark: /* Function */

2015-06-20T14:39:45Z

‎Function

Mark: /* Domain */

2015-06-17T21:17:11Z

‎Domain

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 === Function ===
-yeast cdc14 is required for mitotic exit, though this is not seen in most other species <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>.
+Yeast cdc14 is required for mitotic exit, though this is not seen in most other species <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>.
 Human CDC14A and CDC14B show functional redundancy in double-strand breaks repair <cite>Lin15</cite>, and their unique functions are not well understood.

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 === Domain Architecture ===
-CDC14 has twin DSP phosphatase domains, separated by an alpha helix. The N-terminal domain is a [[pseudophosphatase]]. CDC14 also has a conserved nuclear export sequence (NES) at C-terminal.
+CDC14 has twin DSP phosphatase domains, separated by an alpha helix. The N-terminal domain is a [[pseudophosphatase]]. CDC14 also has a conserved nuclear export sequence (NES) at the C terminus.
-C. elegans cdc-14 has multiple isoforms and the longest one has a THAP domain at C-terminal. The [[Protein_Domain#THAP|THAP domain]] is a DNA-binding domain similar to P element transposase. However, the domain combination is dubious. The spliced ESTs show it is more probably the THAP domain belongs to another gene, by looking into UCSC Genome Browser.
+C. elegans cdc-14 has multiple isoforms and the longest one has a THAP domain at C-terminal. The [[Protein_Domain#THAP|THAP domain]] is a DNA-binding domain similar to P element transposase. However, the domain combination is dubious. ESTs suggest that the the THAP domain may belong to another gene.
-Yeast CDC14 has a C-terminal  sequence (517-551), which not only functions as a nuclear localization signal (NLS) in vivo but also binds to Kap121p (also known as Pse1p), an essential nuclear import carrier (karyopherin/importin) in yeast, in a Gsp1p-GTP-dependent manner in vitro <cite>Kobayashi15</cite>. In human, Kap121 (Pse1) ortholog can be found (IPO5), but human CDC14A and CDC14B have NLSs at N-terminal instead of C-terminal and it is unclear whether IPO5 binds to this region <cite>Gray03</cite>.
+Yeast CDC14 has a C-terminal  sequence (517-551), which acts as a nuclear localization signal (NLS) in vivo and binds to Kap121p (also known as Pse1p), a nuclear import carrier (karyopherin/importin), in a Gsp1p-GTP-dependent manner in vitro <cite>Kobayashi15</cite>. In human, Kap121 (Pse1) ortholog can be found (IPO5), but human CDC14A and CDC14B have NLSs at N-terminal instead of C-terminal and it is unclear whether IPO5 binds to this region <cite>Gray03</cite>.
 === Function ===

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 === Function ===
-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>.
+yeast cdc14 is required for mitotic exit, though this is not seen in most other species <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>.
 Human CDC14A and CDC14B show functional redundancy in double-strand breaks repair <cite>Lin15</cite>, and their unique functions are not well understood.

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 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:  [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_CDC14|Subfamily CDC14]]
-CDC14 subfamily consists of cell cycle genes widely found in eukaryotes with the exception of higher plants.
+CDC14 is a cell cycle phosphatase that dephosphorylates cyclin dependent kinases (CDKs).
 === Evolution ===
-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. Vertebrates have two members, CDC14A and CDC14B. Many primates have an additional CDC14C <cite>Rosso</cite>, though its functional relevance in human is not clear, as it may be a pseudogene.
-=== Domain ===
+=== Domain Architecture ===
-The CDC14 subfamily has two tandem structural equivalent domains linked by an alpha helix. Both domains have a DSP fold and only the second domain is catalytic active. CDC14 also has a conserved nuclear export sequence (NES) at C-terminal.
+CDC14 has twin DSP phosphatase domains, separated by an alpha helix. The N-terminal domain is a [[pseudophosphatase]]. CDC14 also has a conserved nuclear export sequence (NES) at C-terminal.
 C. elegans cdc-14 has multiple isoforms and the longest one has a THAP domain at C-terminal. The [[Protein_Domain#THAP|THAP domain]] is a DNA-binding domain similar to P element transposase. However, the domain combination is dubious. The spliced ESTs show it is more probably the THAP domain belongs to another gene, by looking into UCSC Genome Browser.
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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>.
-Human has two CDC14s, CDC14A and CDC14B. They have shown functional redundancy in double-strand breaks repair <cite>Lin15</cite>. But, it is unclear whether they are functionally redundant in other bio processes.
+Human CDC14A and CDC14B show functional redundancy in double-strand breaks repair <cite>Lin15</cite>, and their unique functions are not well understood.
 ===== Yeast CDC14 =====
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 #Mocciaro10 pmid=20720150
 #Miller15 pmid=26085509
 </biblio>

@@ Line 27: / Line 27: @@
 #Gray03 pmid=12853468
 #Kobayashi15 pmid=26022122
 #Mocciaro10 pmid=20720150
 #Miller15 pmid=26085509
 </biblio>