Phosphatase Subfamily PDPc - Revision history

Gerard: /* Functions */

2017-03-04T01:19:21Z

‎Functions

Gerard: /* Functions */

2017-03-04T01:17:39Z

‎Functions

Gerard at 01:15, 4 March 2017

2017-03-04T01:15:19Z

Gerard at 01:10, 4 March 2017

2017-03-04T01:10:54Z

Mark at 07:58, 6 June 2015

2015-06-06T07:58:06Z

Mark: Mark moved page Phosphatase Subfamily PDP to Phosphatase Subfamily PDPc

2015-06-06T07:57:49Z

Mark moved page Phosphatase Subfamily PDP to Phosphatase Subfamily PDPc

Mark: Created page with "Phosphatase Classification: Fold PPM (PP2C): Superfamily PPM (PP2C): Phosphatase_Fami..."

2015-06-06T06:30:59Z

Created page with "Phosphatase Classification: Fold PPM (PP2C): Superfamily PPM (PP2C): Phosphatase_Fami..."

New page

[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_PPM|Fold PPM (PP2C)]]: [[Phosphatase_Superfamily_PPM|Superfamily PPM (PP2C)]]: [[Phosphatase_Family_PPM|Family PPM (PP2C)]]: [[Phosphatase_Subfamily_PDP|Subfamily PDP]]

=== Evolution ===

=== Domain ===

=== Functions ===
Pyruvate dehydrogenase phosphatase is a heterodimer consisting of catalytic and regulatory subunits.

=== References ===

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 === Functions ===
-The subfamily encodes the catalytic subunit of [http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase pyruvate dehydrogenase] phosphatase complex, which is a heterodimer consisting of catalytic and regulatory subunits. Its substrate PDC is crucial for glucose homeostasis in mammalian cells. The PDC is regulated by [http://kinase.com/wiki/index.php/Kinase_Family_PDHK Pyruvate Dehydrogenase Kinases] and PDPs through inhibitory serine phosphorylation. Because of its critical role in regulating PDC, it is not surprising that PDP1 deficiency may cause severe clinical course. Null mutation caused a lethal infantile phenotype <cite>Cameron09</cite>.
+The subfamily encodes the catalytic subunit of [http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase pyruvate dehydrogenase] phosphatase complex, which is a heterodimer consisting of catalytic and regulatory subunits. Its substrate, the [https://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_complex pyruvate dehydrogenase complex] (PDC) is crucial for glucose homeostasis in mammalian cells. The PDC is regulated by [http://kinase.com/wiki/index.php/Kinase_Family_PDHK Pyruvate Dehydrogenase Kinases] and PDPs through inhibitory serine phosphorylation. Because of its critical role in regulating PDC, it is not surprising that PDP1 deficiency may cause severe clinical course. Null mutation caused a lethal infantile phenotype <cite>Cameron09</cite>.
 The subfamily is conserved in its mitochondria localization and phosphatase activity towards PD, as shown in both vertebrates <cite>Caruso01</cite> and yeast <cite>KrauseBuchholz06</cite>.

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 The two human phosphatases of PDP subfamily PDP1 and PDP2 are widely expressed in different tissues according to the RNA-seq data from GTEx. Human PDP1 are expressed at a higher level than PDP2 (see [http://www.gtexportal.org/home/gene/PDP1 here for PDP1] and [http://www.gtexportal.org/home/gene/PDP2 here for PDP2]). PDP1 is slightly more abundant in ardrenal gland, some parts of brain, heart, and testis than other tissues.
-Human PDPs are regulated by tyrosine phosphorylation. Human PDP1 and PDP2 were phosphorylated and activated by PKCδ upon insulin stimulation <cite>Caruso01</cite>. There are multiple tyrosine positions can be phosphorylated, such as Tyr-94 <cite>Shan14</cite>, Tyr-381 <cite>Fan14</cite>, Tyr-79, Tyr-46. The phosphorylation at different positions can lead to different effects on PD complex phosphorylation state <cite>Fan14, Shan14</cite>.
+Human PDPs are regulated by tyrosine phosphorylation. There are multiple tyrosine positions can be phosphorylated, such as Tyr-94 <cite>Shan14</cite>, Tyr-381 <cite>Fan14</cite>, Tyr-79, Tyr-46. The phosphorylation at different positions can lead to different effects on PD complex phosphorylation state <cite>Fan14, Shan14</cite>. Human PDP1 and PDP2 were phosphorylated and activated by PKCδ upon insulin stimulation <cite>Caruso01</cite>.
 In addition to function as PD phosphatase, fruit fly PDP directly dephosphorylates Smad <cite>Hong06</cite>.

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 === Evolution of pyruvate dehydrogenase (PD) phosphatase, PD kinase (PDK) and PD complex (PDC) ===
-The PDPc subfamily is found in most eukaryotes (see [http://resdev.gene.com/gOrtholog/view/cluster/MC0001235/overview internal database]. But, the regulatory subunit of PD phosphatase (PDP), [http://www.ncbi.nlm.nih.gov/gene/55066 PDPR] in human, is mostly found in eumetazoa (see [http://resdev.gene.com/gOrtholog/view/cluster/MC0005093/overview internal database]. The kinase human PDK1/2/3/4 are found almost in all eukaryotes. The substrate human PD complex has two subunits: alpha subunit encoded by PDHA1 and PDHA2, and beta subunit encoded by PDHB. Both subunits are found almost all eukaryotes.
+The PDPc subfamily is found in most eukaryotes (see [http://resdev.gene.com/gOrtholog/view/cluster/MC0001235/overview internal database], though it's regulatory subunit, [http://www.ncbi.nlm.nih.gov/gene/55066 PDPR], is mostly found in eumetazoa (see [http://resdev.gene.com/gOrtholog/view/cluster/MC0005093/overview internal database]. The opposing [http://kinase.com/wiki/index.php/Kinase_Family_PDHK Pyruvate Dehydrogenase Kinase] family is found in almost all eukaryotes. The substrate human PD complex has two subunits: alpha (PDHA1 or PDHA2), and beta (PDHB). Both subunits are found almost all eukaryotes.
 === Domain ===
-The subfamily PDPc has single structural domain, the phosphatase domain. It is supposed to have a mitochondria targeting sequence (MTS), but no conserved MTS is found by computational prediction using [http://ihg.gsf.de/ihg/mitoprot.html MitoProt].
+PDPc has single structural domain, the phosphatase domain. It is thought to have a mitochondria targeting sequence (MTS), but no conserved MTS is found by computational prediction using [http://ihg.gsf.de/ihg/mitoprot.html MitoProt].
 === Functions ===

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 __NOTOC__
-[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_PPM|Fold PPM (PP2C)]]: [[Phosphatase_Superfamily_PPM|Superfamily PPM (PP2C)]]: [[Phosphatase_Family_PPM|Family PPM (PP2C)]]: [[Phosphatase_Subfamily_PDPc|Subfamily PDPc]]
+[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_PPM|Fold PPM]]: [[Phosphatase_Superfamily_PPM|Superfamily PPM]]: [[Phosphatase_Family_PPM|Family PPM]]: [[Phosphatase_Subfamily_PDPc|Subfamily PDPc]]
 === Evolution of pyruvate dehydrogenase (PD) phosphatase, PD kinase (PDK) and PD complex (PDC) ===
@@ Line 9: / Line 9: @@
 === Functions ===
-The subfamily encodes the catalytic subunit of [http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase pyruvate dehydrogenase] phosphatase complex, which is a heterodimer consisting of catalytic and regulatory subunits. Its substrate PDC is crucial for glucose homeostasis in mammalian cells. The PDC is regulated by PDKs and PDPs through inhibitory serine phosphorylation. Because of its critical role in regulating PDC, it is not surprising that PDP1 deficiency may cause sever clinical course. Null mutation caused a lethal infantile phenotype <cite>Cameron09</cite>.
+The subfamily encodes the catalytic subunit of [http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase pyruvate dehydrogenase] phosphatase complex, which is a heterodimer consisting of catalytic and regulatory subunits. Its substrate PDC is crucial for glucose homeostasis in mammalian cells. The PDC is regulated by [http://kinase.com/wiki/index.php/Kinase_Family_PDHK Pyruvate Dehydrogenase Kinases] and PDPs through inhibitory serine phosphorylation. Because of its critical role in regulating PDC, it is not surprising that PDP1 deficiency may cause severe clinical course. Null mutation caused a lethal infantile phenotype <cite>Cameron09</cite>.
 The subfamily is conserved in its mitochondria localization and phosphatase activity towards PD, as shown in both vertebrates <cite>Caruso01</cite> and yeast <cite>KrauseBuchholz06</cite>.

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