Phosphatase Subfamily DSP12 - Revision history

Gerard at 00:20, 26 October 2016

2016-10-26T00:20:08Z

Gerard at 02:20, 9 March 2016

2016-03-09T02:20:39Z

Mark at 21:25, 1 July 2015

2015-07-01T21:25:55Z

Mark: Created page with "NOTOC Phosphatase Classification: Fold CC1: Superfamily CC1: Phosphatase_Family_..."

2015-02-27T19:43:54Z

Created page with "__NOTOC__ Phosphatase Classification: Fold CC1: Superfamily CC1: Phosphatase_Family_..."

New page

__NOTOC__
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_DSP12|Subfamily DSP12]]

DSP12 is a subfamily conserved throughout unikonts, but its function is poorly understood.

=== Evolution ===
DSP12 is conserved throughout unikonts and usually a single copy in each genome.

=== Domain ===
DSP12 has two domains: phosphatase domain and C-terminal Zinc binding domain. Zinc binding domain is dispensable for in vitro phosphatase activity but is essential for function in vivo. There is a phosphorylation site in Zinc binding domain, serine 335. The phosphorylation regulates subcellular targeting of hYVH1 and augments the DUSP12 G2/M phenotype <cite>Kozarova11</cite>. The Zinc binding domain may act as a redox sensor to impede the active site cysteine from inactivating oxidation <cite>Bonham09</cite>.

=== Function ===
The function of human DUSP12 is poorly understood, particularly in the aspect of its substrate. It interacts with Hsp70 and prevents heat-shock-induced cell death. This function is dependent on its phosphatase catalytic activity, since catalytically inactive DUSP12 is unable to interact with Hsp70 <cite>Sharda09</cite>. Human DUSP12 modulates cell cycle progression, which is mediated by its C-terminal zinc-binding domain. Similarly, in yeast, YVH1 which is human DUSP12 orthologs, regulates cell growth and morphogenesis <cite>Beeser00</cite>, and these functions do not map to the phosphatase domain, but to the C-terminal Zinc binding domain <cite>Beeser00, Muda99, Cain11</cite>. Yeast YVH1 participates in 60S ribosome maturation in a phosphatase-independent manner <cite>Kemmler09, Lo09</cite>.

In addition, human DUSP12 has been shown to be a putative oncogene <cite>Cain11</cite> and contribute to type 2 diabetes susceptibility in Caucasians <cite>Das06</cite>.

=== References ===
<biblio>
#Beeser00 pmid=10852885
#Bonham09 pmid=19567874
#Cain11 pmid=21556130
#Das06 pmid=16936214
#Kemmler09 pmid=19797079
#Kozarova11 pmid=21521943
#Lo09 pmid=19797078
#Muda99 pmid=10446167
#Sharda09 pmid=18973475
</biblio>

@@ Line 8: / Line 8: @@
 === Domain ===
-DSP12 has an N-terminal phosphatase domain and a C-terminal zinc binding domain. Rat DUSP12 has dual-specificity catalytic activity <cite>Munoz-Alonso</cite> and Drosophila DMKP-4 has activity on the synthetic substrate pNPP <cite>Sun</cite>.
+DSP12 has an N-terminal phosphatase domain and a C-terminal zinc binding domain. Rat DUSP12 has dual-specificity catalytic activity <cite>Munoz-Alonso</cite> and both human DUSP12 and Drosophila DMKP-4 have in vitro activity on the synthetic substrate pNPP <cite>Muda99, Sun</cite>.
 The zinc binding domain is dispensable for in vitro phosphatase activity but is essential for function in vivo. There is a phosphorylation site in Zinc binding domain, serine 335. The phosphorylation regulates subcellular targeting of DUSP12 and augments the DUSP12 G2/M phenotype <cite>Kozarova11</cite>. The Zinc binding domain may act as a redox sensor to impede the active site cysteine from inactivating oxidation <cite>Bonham09</cite>.

@@ Line 2: / Line 2: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:  [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_DSP12|Subfamily DSP12]]
-DSP12 is a subfamily conserved throughout unikonts, but its function is poorly understood.
+DSP12 is a unikont phosphatase with roles in heat shock response and cell cycle.
 === Evolution ===
-DSP12 is conserved throughout unikonts and usually a single copy in each genome.
+DSP12 is conserved throughout unikonts and usually a single copy in each genome, including human DUSP12 and yeast YVH1.
 === Domain ===
-DSP12 has two domains: phosphatase domain and C-terminal Zinc binding domain. Zinc binding domain is dispensable for in vitro phosphatase activity but is essential for function in vivo. There is a phosphorylation site in Zinc binding domain, serine 335. The phosphorylation regulates subcellular targeting of hYVH1 and augments the DUSP12 G2/M phenotype <cite>Kozarova11</cite>. The Zinc binding domain may act as a redox sensor to impede the active site cysteine from inactivating oxidation <cite>Bonham09</cite>.
+DSP12 has an N-terminal phosphatase domain and a C-terminal zinc binding domain. Rat DUSP12 has dual-specificity catalytic activity <cite>Munoz-Alonso</cite> and Drosophila DMKP-4 has activity on the synthetic substrate pNPP <cite>Sun</cite>.
-=== Function ===
+The zinc binding domain is dispensable for in vitro phosphatase activity but is essential for function in vivo. There is a phosphorylation site in Zinc binding domain, serine 335. The phosphorylation regulates subcellular targeting of DUSP12 and augments the DUSP12 G2/M phenotype <cite>Kozarova11</cite>. The Zinc binding domain may act as a redox sensor to impede the active site cysteine from inactivating oxidation <cite>Bonham09</cite>.
-The function of human DUSP12 is poorly understood, particularly in the aspect of its substrate. It interacts with Hsp70 and prevents heat-shock-induced cell death. This function is dependent on its phosphatase catalytic activity, since catalytically inactive DUSP12 is unable to interact with Hsp70 <cite>Sharda09</cite>. Human DUSP12 modulates cell cycle progression, which is mediated by its C-terminal zinc-binding domain. Similarly, in yeast, YVH1 which is human DUSP12 orthologs, regulates cell growth and morphogenesis <cite>Beeser00</cite>, and these functions do not map to the phosphatase domain, but to the C-terminal Zinc binding domain <cite>Beeser00, Muda99, Cain11</cite>. Yeast YVH1 participates in 60S ribosome maturation in a phosphatase-independent manner <cite>Kemmler09, Lo09</cite>.
-In addition, human DUSP12 has been shown to be a putative oncogene <cite>Cain11</cite> and contribute to type 2 diabetes susceptibility in Caucasians <cite>Das06</cite>.
+=== Functions ===
-YVH1, yeast's DSP12, is required for pre-autophagosomal structure formation after TORC1 inactivation <cite>Yeasmin15</cite>.
+Human DUSP12 is downregulated during brown fat development, and overexpression blocks adipogenesis <cite>Choi</cite >, while C. elegans C24F3.2 was found in an RNAi screen for genes whose knockdown increased fat content <cite>Ashrafi</cite>. Rat DUSP12 (GKAP) dephosphyorylates glucokinase <cite>Munoz-Alonso</cite>, and human DUSP12 is weakly genetically associated with type 2 diabetes <cite>Das06</cite>.
 === References ===
 <biblio>
 #Beeser00 pmid=10852885
 #Bonham09 pmid=19567874
 #Cain11 pmid=21556130
 #Das06 pmid=16936214
 #Kemmler09 pmid=19797079
 #Kozarova11 pmid=21521943
 #Lo09 pmid=19797078
 #Muda99 pmid=10446167
 #Sharda09 pmid=18973475
 #Yeasmin15 pmid=26125457
 </biblio>

Phosphatase Subfamily DSP12 - Revision history

Gerard at 00:20, 26 October 2016

Gerard at 02:20, 9 March 2016

Mark at 21:25, 1 July 2015

Mark: Created page with "__NOTOC__ Phosphatase Classification: Fold CC1: Superfamily CC1: Phosphatase_Family_..."

Mark: Created page with "NOTOC Phosphatase Classification: Fold CC1: Superfamily CC1: Phosphatase_Family_..."