Phosphatase Subfamily PGP - Revision history

Gerard at 23:59, 13 April 2017

2017-04-13T23:59:14Z

Gerard: /* Functions */

2016-05-16T00:37:49Z

‎Functions

Mark: /* Domain */

2015-06-26T19:08:01Z

‎Domain

Mark: /* Domain */

2015-06-26T19:04:08Z

‎Domain

Mark at 20:20, 21 May 2015

2015-05-21T20:20:37Z

Gerard at 02:32, 22 March 2015

2015-03-22T02:32:56Z

Mark: /* Function */

2015-03-22T01:31:25Z

‎Function

Mark at 01:30, 22 March 2015

2015-03-22T01:30:50Z

Mark: /* Evolution */

2015-03-22T01:25:52Z

‎Evolution

Mark: /* Function */

2015-03-22T01:16:26Z

‎Function

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 === Evolution ===
-PGP is found in most eukaryotes, typically in a single copy. Vertebrates encode two members: PGP and PDXP.
+PGP is found in most eukaryotes, typically in a single copy <cite>Chen</cite>. Vertebrates encode two members: PGP and PDXP.
 === Domain ===
@@ Line 25: / Line 25: @@
 === References ===
 <biblio>
 #Gao94 pmid=8132548
 #Gohla05 pmid=15580268

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 * 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 <cite>Gao94, Jang03, Kim05</cite> and an important biomarker measures B6 status <cite>Ueland15</cite>.
-* Cofilin. PDXP dephosphorylates cofilin at serine, regulating assembly and disassembly of actin filaments <cite>Gohla05, Huang08, Kestler14</cite>.  [[Phosphatase_Subfamily_Slingshot|slingshot]], also dephosphorylates cofilin.
+* Cofilin. PDXP dephosphorylates cofilin at serine, regulating assembly and disassembly of actin filaments <cite>Gohla05, Huang08, Kestler14</cite>.  [[Phosphatase_Subfamily_Slingshot|slingshot]] also dephosphorylates cofilin.
 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 substrates are unknown. It also has a conserved phosphoglycolate phosphatase activity.

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 === Domain ===
-PGPs have a single HAD-fold domain. C. elegans PGP (K02D10.1) has at least three alternative splicing isoforms. One of the isoforms, supported by spliced ESTs, has a [http://pfam.xfam.org/family/PF07978.9 NIPSNAP domain] at C-terminal (another two isoforms encode solely HAD and NIPSNAP domain, respectively).
+PGPs have a single HAD-fold domain.
 === Functions ===

@@ Line 8: / Line 8: @@
 === Domain ===
-PGPs have a single HAD-fold domain.
+PGPs have a single HAD-fold domain. C. elegans PGP (K02D10.1) has at least three alternative splicing isoforms. One of the isoforms, supported by spliced ESTs, has a [http://pfam.xfam.org/family/PF07978.9 NIPSNAP domain] at C-terminal (another two isoforms encode solely HAD and NIPSNAP domain, respectively).
 === Functions ===

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 PDXP (Chronophin) is abundantly expressed in brain <cite>Jang03</cite> (see also [http://www.gtexportal.org/home/gene/PDXP 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 <cite>Gao94, Jang03, Kim05</cite>.
+* 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 <cite>Gao94, Jang03, Kim05</cite> and an important biomarker measures B6 status <cite>Ueland15</cite>.
 * Cofilin. PDXP dephosphorylates cofilin at serine, regulating assembly and disassembly of actin filaments <cite>Gohla05, Huang08, Kestler14</cite>.  [[Phosphatase_Subfamily_Slingshot|slingshot]], also dephosphorylates cofilin.
@@ Line 31: / Line 31: @@
 #Seifried14 pmid=24338473
 #Tuleva98 pmid=9561742
 </biblio>

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 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_NagD|Family NagD]]: [[Phosphatase_Subfamily_PGP|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.
+PGP is ubiquitous in eukaryotes and has been reported to act on both proteins and small molecules.
 === 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.
+PGP is found in most eukaryotes, typically in a single copy. Vertebrates encode two members: PGP and PDXP.
 === Domain ===
-The PGP subfamily has a single domain: HAD domain.
+PGPs have a single HAD-fold domain.
-=== Function ===
+=== Functions ===
 PDXP (Chronophin) is abundantly expressed in brain <cite>Jang03</cite> (see also [http://www.gtexportal.org/home/gene/PDXP 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 <cite>Gao94, Jang03, Kim05</cite>.
-* Protein cofilin. PDXP dephosphorylates cofilin at serine, therefore regulating assembly and disassembly of actin filaments <cite>Gohla05, Huang08, Kestler14</cite>. It is worthy pointing out that another phosphatse subfamily, [[Phosphatase_Subfamily_Slingshot|slingshot]], also dephosphorylates cofilin.
+* Cofilin. PDXP dephosphorylates cofilin at serine, regulating assembly and disassembly of actin filaments <cite>Gohla05, Huang08, Kestler14</cite>.  [[Phosphatase_Subfamily_Slingshot|slingshot]], also dephosphorylates cofilin.
-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 substrates are unknown. It also has a conserved phosphoglycolate phosphatase activity.
-Yeast has a single member PHO13, which has phosphatase activity on the serines of proteins histone II-A and casein <cite>Tuleva98</cite>.
+The yeast PGP, PHO13, has serine phosphatase activity against histone II-A and casein <cite>Tuleva98</cite>, and also acts on the synthetic small-molecule substrate PNPP ([https://en.wikipedia.org/wiki/Para-Nitrophenylphosphate para-nitrophenyl phosphate]). Deletion of PHO13 increases expression of pentose phosphate pathway genes and allows more efficient use of xylose.
 === References ===