Phosphatase Subfamily STYXL1 - Revision history

Gerard: /* Domain */

2017-07-26T08:05:47Z

‎Domain

Gerard at 23:55, 13 April 2017

2017-04-13T23:55:02Z

Gerard at 21:06, 7 September 2016

2016-09-07T21:06:02Z

Gerard at 20:59, 7 September 2016

2016-09-07T20:59:56Z

Gerard: /* Evolution */

2016-09-07T20:59:27Z

‎Evolution

Gerard: /* Function */

2016-09-07T20:57:31Z

‎Function

Gerard: /* Domain */

2016-09-07T20:53:22Z

‎Domain

Gerard at 21:59, 12 May 2015

2015-05-12T21:59:13Z

Gerard: /* Domain */

2015-05-12T21:58:48Z

‎Domain

Mark at 20:19, 3 March 2015

2015-03-03T20:19:23Z

@@ Line 8: / Line 8: @@
 === Domain ===
-STYXL1 has two domains: an N-terminal rhodanese domain and C-terminal phosphatase domain.
+STYXL1 has an N-terminal rhodanese domain and C-terminal phosphatase domain.
 === Functions ===

@@ Line 5: / Line 5: @@
 === Evolution ===
-STYXL1 is found in [[metazoa]] but lost in [[ecdysozoa]] (arthropods and nematodes). It is usually found in one copy per genome.
+STYXL1 is found in [[metazoa]] but lost in [[ecdysozoa]] (arthropods and nematodes) <cite>Chen</cite>. It is usually found in one copy per genome.
 === Domain ===
@@ Line 22: / Line 22: @@
 <biblio>
 #Barr13 pmid=23163895
 #Flowers pmid=25479605
 #Hinton10 pmid=20180778

@@ Line 16: / Line 16: @@
 STYXL1 also interacts with G3BP-1 (Ras-GTPase activating protein SH3 domain binding protein-1), a key component of stress granules. G3BP1 is an RNA-binding protein with endoribonuclease activity that is recruited to 'stress granules' after stress stimuli. Stress granules are large subcellular structures that serve as sites of mRNA sorting, in which untranslated mRNAs accumulate. A mutant active STYXL1, which has been transformed from pseudophosphatase to phosphatase by restoration of HC of the HCx5R motif, has opposite effects to wild-type STYKL1 (inactive). The active mutant STYXL1 induces stress granules and dephosphorylates G3BP-1. <cite>Hinton10, Barr13</cite>.
 === References ===
 <biblio>
 #Barr13 pmid=23163895
 #Hinton10 pmid=20180778
 #Niemi11 pmid=21262771
 #Niemi14 pmid=24709986
 </biblio>

@@ Line 2: / Line 2: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:  [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_ STYXL1 |Subfamily STYXL1]]
-STYXL1 (MK-STYX) is a pseudophosphatase (catalytically inactive) conserved in metazoan but lost in [[ecdysozoa]]. Two binding partners have been known so far: phosphatase PTPMT1 and a Ras signaling regulator G3BP1.
+STYXL1 (MK-STYX) is a pseudophosphatase (catalytically inactive) conserved in metazoa but lost in ecdysozoa. Two binding partners have been known so far: phosphatase PTPMT1 and a Ras signaling regulator G3BP1.
 === Evolution ===

@@ Line 5: / Line 5: @@
 === Evolution ===
-STYXL1 is found in [[metazoa]] but lost in [[ecdysozoa]] (arthropoda and nematoda). It is usually a copy per genome.
+STYXL1 is found in [[metazoa]] but lost in [[ecdysozoa]] (arthropods and nematodes). It is usually found in one copy per genome.
 === Domain ===

@@ Line 10: / Line 10: @@
 STYXL1 has two domains: an N-terminal rhodanese domain and C-terminal phosphatase domain.
-=== Function ===
+=== Functions ===
 STYXL1 is expressed in most tissues (see [http://www.gtexportal.org/home/gene/STYXL1 GTEx data]).
-STYXL1 physically and genetically interacts with the mitochondrial phosphatase PTPMT1, and suppresses PTPMT1 catalytic activity.  STYXL1 knockdown induces robust chemoresistance to multiple cytotoxic death-inducing agents.  Loss of STYXL1 blocks cytochrome c release, a critical and rate-limiting step in apoptosis.  knockdown of PTPMT1 resensitizes STYXL1 knockdown cells to chemotherapeutics and restores the ability to release cytochrome c. Thus, a model has been proposed that MK-STYX controls apoptosis by negatively regulating PTPMT1 <cite> Niemi11, Niemi14</cite>.
+STYXL1 physically and genetically interacts with the mitochondrial phosphatase PTPMT1, and suppresses PTPMT1 catalytic activity.  STYXL1 knockdown induces robust chemoresistance to multiple cytotoxic death-inducing agents.  Loss of STYXL1 blocks cytochrome c release, a critical and rate-limiting step in apoptosis.  knockdown of PTPMT1 resensitizes STYXL1 knockdown cells to chemotherapeutics and restores the ability to release cytochrome c. This suggests that STYXL1 controls apoptosis by negatively regulating PTPMT1 <cite> Niemi11, Niemi14</cite>.
-STYXL1 also interacts with G3BP-1 (Ras-GTPase activating protein SH3 domain binding protein-1), a key component of stress granules. G3BP1 is an RNA-binding protein with endoribonuclease activity that is recruited to 'stress granules' after stress stimuli. Stress granules are large subcellular structures that serve as sites of mRNA sorting, in which untranslated mRNAs accumulate. Active mutant STYXL1 (active) has opposite effects to wild-type STYKL1 (inactive). The mutant STYXL1 (active) induces stress granules and dephosphorylates G3BP-1. <cite>Hinton10, Barr13</cite>.
+STYXL1 also interacts with G3BP-1 (Ras-GTPase activating protein SH3 domain binding protein-1), a key component of stress granules. G3BP1 is an RNA-binding protein with endoribonuclease activity that is recruited to 'stress granules' after stress stimuli. Stress granules are large subcellular structures that serve as sites of mRNA sorting, in which untranslated mRNAs accumulate. A mutant active STYXL1, which has been transformed from pseudophosphatase to phosphatase by restoration of HC of the HCx5R motif, has opposite effects to wild-type STYKL1 (inactive). The active mutant STYXL1 induces stress granules and dephosphorylates G3BP-1. <cite>Hinton10, Barr13</cite>.
 === References ===