Difference between revisions of "Phosphatase Subfamily PGP"
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In contrast with PDXP, PGP (AUM) is widely expressed in different tissues (see also [http://www.gtexportal.org/home/gene/PGP GTEx] RNA-seq data). PGP is a putative tyrosine-specific phosphatase <cite>Seifried14</cite>, but its physiological substrate needs to be found. | In contrast with PDXP, PGP (AUM) is widely expressed in different tissues (see also [http://www.gtexportal.org/home/gene/PGP GTEx] RNA-seq data). PGP is a putative tyrosine-specific phosphatase <cite>Seifried14</cite>, but its physiological substrate needs to be found. | ||
| − | Yeast has a single member PHO13, which has | + | Yeast has a single member PHO13, which has phosphatase activity on the serines of proteins histone II-A and casein <cite>Tuleva98</cite>. |
=== References === | === References === | ||
Revision as of 01:31, 22 March 2015
Phosphatase Classification: Fold HAD: Superfamily HAD: Family NagD: Subfamily PGP
PGP is ubiquitous in eukaryotes. The two members in human have distinct functions: PDXP (aka chronophin) dephosphorylates protein cofilin on serine residue, as well as pyridoxal 5'-phosphate; PGP is a putative tyrosine-specific protein phosphatase. PDXP is mainly expressed in brain; PGP is widely expressed in different tissues.
Evolution
The PGP subfamily is extremely conserved in eukaryotes, rarely absent from eukaryotic genomes. Human has two members of this subfamily: PGP and PDXP. Specific PGP and PDXP orthologs are found in all vertebrates and likely originate in the vertebrate whole genome duplication.
Domain
The PGP subfamily has a single domain: HAD domain.
Function
PDXP (Chronophin) is abundantly expressed in brain [1] (see also GTEx RNA-seq data). PDXP has two distinct substrates.
- Pyridoxal 5'-phosphate. PDXP was first identified as pyridoxal phosphatase, which catalyzes the dephosphorylation of pyridoxal 5'-phosphate (PLP) and pyridoxine 5'-phosphate. PLP is the active form of vitamin B6 that acts as a coenzyme in maintaining biochemical homeostasis [1, 2, 3].
- Protein cofilin. PDXP dephosphorylates cofilin at serine, therefore regulating assembly and disassembly of actin filaments [4, 5, 6]. It is worthy pointing out that another phosphatse subfamily, slingshot, also dephosphorylates cofilin.
In contrast with PDXP, PGP (AUM) is widely expressed in different tissues (see also GTEx RNA-seq data). PGP is a putative tyrosine-specific phosphatase [7], but its physiological substrate needs to be found.
Yeast has a single member PHO13, which has phosphatase activity on the serines of proteins histone II-A and casein [8].
References
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- Error fetching PMID 24338687:
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- Error fetching PMID 9561742:
