Difference between revisions of "Phosphatase Subfamily PPM1G"
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=== Functions === | === Functions === | ||
| − | + | Like known PPM (PP2Cs), recombinant PPM1G requires Mg2+ or Mn2+ for activity <cite>Travis97</cite>. Human PPM1G has the substrates below: | |
| − | + | ||
| − | Like known PPM (PP2Cs), recombinant PPM1G requires Mg2+ or Mn2+ for activity <cite>Travis97</cite>. | + | |
| − | + | ||
| − | Human PPM1G has the substrates below: | + | |
* Deubiquitylation enzyme USP7/HAUSP. PPM1G dephosphorylates USP7S which leads to USP7S downregulation, followed by Mdm2 downregulation and accumulation of p53 <cite>Khoronenkova12</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 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>. | ||
| − | 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. | + | 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. |
| + | |||
| + | 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 is associated with alcohol use disorder <cite>Ruggeri15</cite>. | + | Besides, PPM1G is associated with alcohol use disorder <cite>Ruggeri15</cite>. |
=== References === | === References === | ||
Revision as of 00:18, 1 June 2015
Phosphatase Classification: Fold PPM (PP2C): Superfamily PPM (PP2C): Family PPM (PP2C): Subfamily PPM1G
Evolution
PPM1G emerged in holozoa, usually single copy per genome. Human has a single PPM1G (PP2CG/PP2Cγ/FIN13).
Domain
PPM1G has a single structural domain, the phosphatase domain of PPM fold. Unlike any other known phosphatase, PPM1G has a highly acidic domain: 75% of the 54 residues are glutamate or aspartate [1].
Functions
Like known PPM (PP2Cs), recombinant PPM1G requires Mg2+ or Mn2+ for activity [1]. Human PPM1G has the substrates below:
- Deubiquitylation enzyme USP7/HAUSP. PPM1G dephosphorylates USP7S which leads to USP7S downregulation, followed by Mdm2 downregulation and accumulation of p53 [2].
- 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 [3].
Northern blot analysis shows that human PPM1G is widely expressed, and is most abundant in testis, skeletal muscle, and heart [1]. RNA-seq data from GTEx also shows its broad expression in different tissues and particularly abundant in testis.
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 [4]. It is unclear whether PPM1G dephosphorylates WWP1 or WWP2.
Besides, PPM1G is associated with alcohol use disorder [5].
References
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