Phosphatase Subfamily Slingshot - Revision history

Gerard: /* Domain */

2017-07-23T18:36:58Z

‎Domain

Gerard at 15:39, 22 March 2017

2017-03-22T15:39:06Z

Gerard at 15:35, 22 March 2017

2017-03-22T15:35:41Z

Gerard: /* Domain */

2017-03-22T15:34:39Z

‎Domain

Gerard at 04:45, 30 April 2015

2015-04-30T04:45:12Z

Gerard: /* Function */

2015-04-30T04:43:12Z

‎Function

Gerard: /* Evolution */

2015-04-30T04:39:22Z

‎Evolution

Mark at 03:57, 27 February 2015

2015-02-27T03:57:23Z

Mark at 02:15, 27 February 2015

2015-02-27T02:15:51Z

Mark at 02:14, 27 February 2015

2015-02-27T02:14:07Z

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 Slingshot is found across [[holozoa]], but absent from nematodes.
-=== Domain ===
+=== Domain Architecture===
-Slingshot has three domains defined experimentally: A domain (1-124), B domain (125-308), phosphatase domain (309-450) and Serine-enriched region close to C-terminus (numbering from human SSH1) <cite>Kurita08</cite>. The B domain includes the Pfam domain DEK_C. The A domain is required for the F-actin-mediated activation of SSH1 and therefore may mediate slingshot binding to actin. F-actin increased the cofilin-phosphatase activity of SSH1 more than 1200-fold. The B domain and phosphatase domain are indispensable for phosphorylated-cofilin (P-cofilin) binding. The phosphatase domain alone is sufficient for the phosphatase activity toward p-nitrophenyl phosphate (pNPP)  <cite>Kurita08</cite>. The motifs LHKACE (AA 185–190) in the B domain and LKRSHS (AA 973–978) in the S domain of SSH1 may also contribute to F-actin binding <cite>Yamamoto06</cite>.
+Slingshot has four domains defined experimentally: A domain (1-124), B domain (125-308), phosphatase domain (309-450) and Serine-enriched region close to the C-terminus (numbering from human SSH1) <cite>Kurita08</cite>. The B domain includes the Pfam domain DEK_C. The A domain is required for the F-actin-mediated activation of SSH1 and therefore may mediate slingshot binding to actin. F-actin increased the cofilin-phosphatase activity of SSH1 more than 1200-fold. The B domain and phosphatase domain are indispensable for phosphorylated-cofilin (P-cofilin) binding. The phosphatase domain alone is sufficient for the phosphatase activity toward p-nitrophenyl phosphate (pNPP)  <cite>Kurita08</cite>. The motifs LHKACE (AA 185–190) in the B domain and LKRSHS (AA 973–978) in the S domain of SSH1 may also contribute to F-actin binding <cite>Yamamoto06</cite>.
 === Function ===

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 === Domain ===
-Slingshot has three domains defined experimentally: A domain (1-124), B domain (125-308), phosphatase domain (309-450) and Serine-enriched region close to C-terminus (numbering from human SSH1) <cite>Kurita08</cite>. The B domain includes the Pfam domain DEK_C
+Slingshot has three domains defined experimentally: A domain (1-124), B domain (125-308), phosphatase domain (309-450) and Serine-enriched region close to C-terminus (numbering from human SSH1) <cite>Kurita08</cite>. The B domain includes the Pfam domain DEK_C. The A domain is required for the F-actin-mediated activation of SSH1 and therefore may mediate slingshot binding to actin. F-actin increased the cofilin-phosphatase activity of SSH1 more than 1200-fold. The B domain and phosphatase domain are indispensable for phosphorylated-cofilin (P-cofilin) binding. The phosphatase domain alone is sufficient for the phosphatase activity toward p-nitrophenyl phosphate (pNPP)  <cite>Kurita08</cite>. The motifs LHKACE (AA 185–190) in the B domain and LKRSHS (AA 973–978) in the S domain of SSH1 may also contribute to F-actin binding <cite>Yamamoto06</cite>.
-A domain is required for the F-actin-mediated activation of SSH1 and therefore may mediate slingshot binding to actin. F-actin increased the cofilin-phosphatase activity of SSH1 more than 1200-fold. B domain and phosphatase domain are indispensable for phosphorylated-cofilin (P-cofilin) binding. The phosphatase domain alone is sufficient for the phosphatase activity toward p-nitrophenyl phosphate (pNPP), indicating that the SSH-N domain is not essential for the basal phosphatase activity of SSH1 <cite>Kurita08</cite>. Besides, motifs LHKACE (amino acids 185–190) in the B domain and LKRSHS (amino acids 973–978) in the S domain of SSH1 may also contribute to F-actin binding <cite>Yamamoto06</cite>.
 === Function ===
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 === Regulation ===
-Slingshot is regulated by protein kinase D (PKD), which phosphorylates serines 937 and 978 and therefore regulates human SSH1 subcellular localization by binding of 14-3-3 proteins <cite>Peterburs09</cite>. PKD also phosphorylates serine 402 that impedes phosphatase activity of human SSH1 <cite>Barisic11</cite>. 14-3-3zeta/tau heterodimers regulate Slingshot activity in migrating keratinocytes <cite>Kligys09</cite>. SSH1L is activated by its release from a regulatory complex with 14-3-3zeta protein through the redox-mediated oxidation of 14-3-3zeta <cite>Kim09</cite>.
+Slingshot is regulated by protein kinase D (PKD), which phosphorylates serines 937 and 978 and regulates human SSH1 subcellular localization by binding of 14-3-3 proteins <cite>Peterburs09</cite>. PKD also phosphorylates serine 402 to inhibit phosphatase activity  <cite>Barisic11</cite>. 14-3-3zeta/tau heterodimers regulate Slingshot activity in migrating keratinocytes <cite>Kligys09</cite>. SSH1 is activated by its release from a regulatory complex with 14-3-3zeta protein through the redox-mediated oxidation of 14-3-3zeta <cite>Kim09</cite>.
 === References ===

@@ Line 8: / Line 8: @@
 === Domain ===
-Slingshot has three domains: A domain (1-124), B domain (125-308), phosphatase domain (309-450) and Serine-enriched region close to C-terminus (numbering from human SSH1).
+Slingshot has three domains defined experimentally: A domain (1-124), B domain (125-308), phosphatase domain (309-450) and Serine-enriched region close to C-terminus (numbering from human SSH1) <cite>Kurita08</cite>. The B domain includes the Pfam domain DEK_C
 A domain is required for the F-actin-mediated activation of SSH1 and therefore may mediate slingshot binding to actin. F-actin increased the cofilin-phosphatase activity of SSH1 more than 1200-fold. B domain and phosphatase domain are indispensable for phosphorylated-cofilin (P-cofilin) binding. The phosphatase domain alone is sufficient for the phosphatase activity toward p-nitrophenyl phosphate (pNPP), indicating that the SSH-N domain is not essential for the basal phosphatase activity of SSH1 <cite>Kurita08</cite>. Besides, motifs LHKACE (amino acids 185–190) in the B domain and LKRSHS (amino acids 973–978) in the S domain of SSH1 may also contribute to F-actin binding <cite>Yamamoto06</cite>.
 === Function ===

@@ Line 8: / Line 8: @@
 === Domain ===
-Slingshot has three domains: A domain (1-124), B domain (125-308), phosphatase domain (309-450) and Serine-enriched region close to C-terminus (positioned by human SSH1).
+Slingshot has three domains: A domain (1-124), B domain (125-308), phosphatase domain (309-450) and Serine-enriched region close to C-terminus (numbering from human SSH1).
 A domain is required for the F-actin-mediated activation of SSH1 and therefore may mediate slingshot binding to actin. F-actin increased the cofilin-phosphatase activity of SSH1 more than 1200-fold. B domain and phosphatase domain are indispensable for phosphorylated-cofilin (P-cofilin) binding. The phosphatase domain alone is sufficient for the phosphatase activity toward p-nitrophenyl phosphate (pNPP), indicating that the SSH-N domain is not essential for the basal phosphatase activity of SSH1 <cite>Kurita08</cite>. Besides, motifs LHKACE (amino acids 185–190) in the B domain and LKRSHS (amino acids 973–978) in the S domain of SSH1 may also contribute to F-actin binding <cite>Yamamoto06</cite>.

@@ 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_Slingshot|Subfamily Slingshot]]
-Slingshot, a subfamily conserved in holozoan but lost in nematodes, regulates [http://en.wikipedia.org/wiki/Cofilin cofilin] phosphorylation with LIMK kinase subfamily.
+Slingshot regulates [http://en.wikipedia.org/wiki/Cofilin cofilin] phosphorylation with LIMK kinase subfamily.
 === Evolution ===
 Slingshot is found across [[holozoa]], but absent from nematodes.
 === Domain ===
 Slingshot has three domains: A domain (1-124), B domain (125-308), phosphatase domain (309-450) and Serine-enriched region close to C-terminus (positioned by human SSH1).
 A domain is required for the F-actin-mediated activation of SSH1 and therefore may mediate slingshot binding to actin. F-actin increased the cofilin-phosphatase activity of SSH1 more than 1200-fold. B domain and phosphatase domain are indispensable for phosphorylated-cofilin (P-cofilin) binding. The phosphatase domain alone is sufficient for the phosphatase activity toward p-nitrophenyl phosphate (pNPP), indicating that the SSH-N domain is not essential for the basal phosphatase activity of SSH1 <cite>Kurita08</cite>. Besides, motifs LHKACE (amino acids 185–190) in the B domain and LKRSHS (amino acids 973–978) in the S domain of SSH1 may also contribute to F-actin binding <cite>Yamamoto06</cite>.
@@ Line 19: / Line 17: @@
 === Regulation ===
 Slingshot is regulated by protein kinase D (PKD), which phosphorylates serines 937 and 978 and therefore regulates human SSH1 subcellular localization by binding of 14-3-3 proteins <cite>Peterburs09</cite>. PKD also phosphorylates serine 402 that impedes phosphatase activity of human SSH1 <cite>Barisic11</cite>. 14-3-3zeta/tau heterodimers regulate Slingshot activity in migrating keratinocytes <cite>Kligys09</cite>. SSH1L is activated by its release from a regulatory complex with 14-3-3zeta protein through the redox-mediated oxidation of 14-3-3zeta <cite>Kim09</cite>.
 === References ===
 <biblio>
 #Cai07 pmid=17350576

@@ Line 16: / Line 16: @@
 === Function ===
-----
+Slingshot dephosphorylates [http://en.wikipedia.org/wiki/Cofilin cofilin], a ubiquitous actin-binding factor required for the reorganization of actin filaments, in Drosophila and human <cite>Niwa02</cite> (see [http://www.nature.com/nrm/journal/v14/n7/fig_tab/nrm3609_F6.html here] for cofilin function). The three human slingshot genes are significantly different in subcellular distribution, actin-binding activity, phosphatase activity and expression patterns <cite>Ohta02</cite>. [http://en.wikipedia.org/wiki/Coronin Coronin 1B] has also been proposed to be a slingshot substrate <cite>Cai07</cite>.
-Slingshots dephosphorylate [http://en.wikipedia.org/wiki/Cofilin cofilin], a ubiquitous actin-binding factor required for the reorganization of actin filaments, in Drosophila and human <cite>Niwa02</cite> (see [http://www.nature.com/nrm/journal/v14/n7/fig_tab/nrm3609_F6.html here] for cofilin function). In human, there are three members in slingshot subfamily. They are significantly different in subcellular distribution, F-actin-binding activity, specific phosphatase activity and expression patterns, which suggests that they have related but distinct functions in various cellular and developmental events <cite>Ohta02</cite>.
-−
-In addition to substrate cofilin, [http://en.wikipedia.org/wiki/Coronin Coronin 1B] has been proposed to be slingshot's substrate <cite>Cai07</cite>.
 === Regulation ===