Phosphatase Subfamily PPM1G - Revision history

Gerard: /* Domain */

2016-06-08T22:27:51Z

‎Domain

Gerard at 22:21, 8 June 2016

2016-06-08T22:21:18Z

Gerard at 21:55, 8 June 2016

2016-06-08T21:55:35Z

Mark: /* References */

2015-09-22T17:24:59Z

‎References

Mark: /* Functions */

2015-09-22T17:24:42Z

‎Functions

Mark: /* Domain */

2015-06-12T17:59:59Z

‎Domain

Mark at 04:46, 1 June 2015

2015-06-01T04:46:20Z

Mark: /* Functions */

2015-06-01T00:18:59Z

‎Functions

Mark at 05:25, 31 May 2015

2015-05-31T05:25:35Z

Mark: /* Functions */

2015-05-31T04:50:30Z

‎Functions

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 === Domain ===
-PPM1G consists entirely of a PPM fold phosphatase domain. Unlike other phosphatases, PPM1G is highly acidic: 75% of the 54 residues are glutamate or aspartate <cite>Travis97</cite>. The acidic nature is essential for its activity in splicing and interacts with YB-1, a splicesome-associated factor <cite>Allemand07</cite>.
+PPM1G consists almost entirely of a PPM fold phosphatase domain. The phosphatase domain has a highly acidic insert in which 75% of the 54 residues are glutamate or aspartate in human <cite>Travis97</cite>. The acidic insert is essential for its activity in splicing and interacts with YB-1, a splicesome-associated factor <cite>Allemand07</cite>.
 Human PPM1G also has a N-terminal myristoylation site and a predicted C-terminal nuclear localization signaling <cite>Petri07</cite>.

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 * PPM1G binds to 7SK RNA and the kinase inhibitor Hexim1 once P-TEFb kinase has been released from the 7SK small nuclear ribonucleoprotein (7SK snRNP) complex. The P-TEFb kinase phosphorylates RNA Polymerase II (Pol II) after the release from 7SK nRNP complex, therefore regulating transcription elongation <cite>Gudipaty15</cite>.
 * PPM1G is associated with alcohol use disorder <cite>Ruggeri15</cite>.
 === References ===

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 === Evolution ===
-PPM1G emerged in [[holozoa]], usually single copy per genome. Human has a single PPM1G (PP2CG/PP2Cγ/FIN13).
+PPM1G emerged in [[holozoa]]. Human has a single PPM1G (PP2CG/PP2Cγ/FIN13), as do most other organisms.
 === Domain ===
-The PPM1G subfamily has a single structural domain, the phosphatase domain of PPM fold. Unlike any other known phosphatase, PPM1G has a highly acidic domain (AD): 75% of the 54 residues are glutamate or aspartate <cite>Travis97</cite>. The acidic domain is essential for its activity in splicing and interacts with YB-1, a splicesome-associated factor <cite>Allemand07</cite>.
+PPM1G consists entirely of a PPM fold phosphatase domain. Unlike other phosphatases, PPM1G is highly acidic: 75% of the 54 residues are glutamate or aspartate <cite>Travis97</cite>. The acidic nature is essential for its activity in splicing and interacts with YB-1, a splicesome-associated factor <cite>Allemand07</cite>.
 Human PPM1G also has a N-terminal myristoylation site and a predicted C-terminal nuclear localization signaling <cite>Petri07</cite>.
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 === Functions ===
 PPM1G is a nuclear phosphatase <cite>Petri07</cite>. Northern blot analysis shows that human PPM1G is widely expressed, and is most abundant in testis, skeletal muscle, and heart <cite>Travis97</cite>. RNA-seq data from GTEx also shows its broad expression in different tissues and particularly abundant in testis.  Its best known function is involved in splicesome (see below). Like other PPMs (PP2Cs), recombinant PPM1G requires Mg2+ or Mn2+ for activity <cite>Travis97</cite>.  Human PPM1G has the substrates below:
 * Nucleosome-free Histones H2A-H2B. Alternatively, the phosphatase activity and/or substrate specificity of PPM1G might be controlled by binding with histones <cite>Kimura06</cite>.
 * Deubiquitylation enzyme USP7/HAUSP. PPM1G dephosphorylates USP7S which leads to USP7S downregulation, followed by Mdm2 downregulation and accumulation of p53 <cite>Khoronenkova12</cite>.
-* 4E binding protein 1 (4E-BP1). PPM1G regulates protein translation and cell growth by dephosphorylating 4E binding protein 1 (4E-BP1), which binds to translation initiation factor 4E and inhibits cap-dependent translation in a phosphorylation-dependent manner <cite>Liu13</cite>.
+* 4E binding protein 1 (4E-BP1). PPM1G regulates protein translation and cell growth by dephosphorylating 4E-BP1, which binds to translation initiation factor 4E and inhibits cap-dependent translation in a phosphorylation-dependent manner <cite>Liu13</cite>.
-* Survival motor neurons (SMN) complex. PPM1G interacts with and dephosphorylates SMN complex, possibly the components SMN and Gemin3. The dephosphorylation reduces the stability of the SMN complex and its level in nuclear Cajal bodies <cite>Petri07</cite>.
+* Survival motor neurons (SMN) complex. PPM1G interacts with and dephosphorylates the SMN complex, possibly the components SMN and Gemin3. The dephosphorylation reduces the stability of the SMN complex and its level in nuclear Cajal bodies <cite>Petri07</cite>.
-* Splicesome. PPM1G is  a splicing factor modulates alternative splicing of specific pre-mRNAs coregulated by YB-1, a splicesome-associated factor <cite>Allemand07</cite>. It dephosphorylates specific substrates required for the formation of the spliceosome <cite> Murray99 </cite>, but the substrates are unclear <cite>Suh09</cite>. <cite>Allemand07</cite>.
+* Splicesome. PPM1G is a splicing factor that modulates alternative splicing of specific pre-mRNAs coregulated by YB-1, a splicesome-associated factor <cite>Allemand07</cite>. It dephosphorylates specific substrates required for the formation of the spliceosome <cite> Murray99 </cite>, but the substrates are unclear <cite>Suh09, Allemand07</cite>.
 PPM1G may have other functions and/or be involved in other processes:
 * PPM1G inactivates monomeric the E3 ligase WWP2 and promotes the assembly of two E3 ligases WWP2-WWP1 heterodimeric complex <cite>Chaudhary14</cite>. It is unclear whether PPM1G dephosphorylates WWP1 or WWP2.
 * PPM1G binds to 7SK RNA and the kinase inhibitor Hexim1 once P-TEFb kinase has been released from the 7SK small nuclear ribonucleoprotein (7SK snRNP) complex. The P-TEFb kinase phosphorylates RNA Polymerase II (Pol II) after the release from 7SK nRNP complex, therefore regulating transcription elongation <cite>Gudipaty15</cite>.
+* PPM1G is associated with alcohol use disorder <cite>Ruggeri15</cite>.
-Besides, PPM1G is associated with alcohol use disorder <cite>Ruggeri15</cite>.
 === References ===

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 #Allemand07 pmid=17572683
 #Chaudhary14 pmid=25071155
 #Khoronenkova12 pmid=22361354
 #Kimura06 pmid=17074886

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 * Splicesome. PPM1G is  a splicing factor modulates alternative splicing of specific pre-mRNAs coregulated by YB-1, a splicesome-associated factor <cite>Allemand07</cite>. It dephosphorylates specific substrates required for the formation of the spliceosome <cite> Murray99 </cite>, but the substrates are unclear <cite>Suh09</cite>. <cite>Allemand07</cite>.
-PPM1G may have other functions and/or be involved in other processes. PPM1G inactivates monomeric the E3 ligase WWP2 and promotes the assembly of two E3 ligases WWP2-WWP1 heterodimeric complex <cite>Chaudhary14</cite>. It is unclear whether PPM1G dephosphorylates WWP1 or WWP2.
+PPM1G may have other functions and/or be involved in other processes:
 Besides, PPM1G is associated with alcohol use disorder <cite>Ruggeri15</cite>.

← Older revision		Revision as of 04:50, 31 May 2015
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	=== Functions ===		=== Functions ===
		+	PPM1G inactivates monomeric WWP2 and promotes the assembly of WWP2-WWP1 heterodimeric complex <cite>Chaudhary14</cite>.
		+
	PPM1G is associated with alcohol use disorder <cite>Ruggeri15</cite>.		PPM1G is associated with alcohol use disorder <cite>Ruggeri15</cite>.