Phosphatase Subfamily MTMR14 - Revision history

Gerard at 23:03, 8 September 2016

2016-09-08T23:03:47Z

Gerard at 21:59, 8 September 2016

2016-09-08T21:59:32Z

Gerard: /* Evolution */

2016-09-08T21:42:58Z

‎Evolution

Mark: /* Domain Structure */

2016-03-17T19:57:30Z

‎Domain Structure

Mark at 17:45, 6 October 2015

2015-10-06T17:45:48Z

Mark at 22:23, 31 December 2014

2014-12-31T22:23:17Z

Mark at 18:16, 31 December 2014

2014-12-31T18:16:07Z

Mark: /* Evolution */

2014-12-31T18:11:59Z

‎Evolution

Mark: /* References */

2014-12-31T18:10:46Z

‎References

Mark: /* Catalytic activity and functions */

2014-12-31T18:08:33Z

‎Catalytic activity and functions

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 ===Domain Structure===
-MTMR14 in eumetazoa has a conserved domain combination: a PH/GRAM domain and an active phosphatase domain. It may have a coiled-coil domain, but it is much weaker compared with other myotubularins using coiled-coil detection programs [http://www.ch.embnet.org/software/COILS_form.html COILS] and [http://paircoil2.csail.mit.edu/paircoil2.html PAIRCOIL2].
+MTMR14 in eumetazoa has a conserved domain combination: a PH/GRAM domain and an active phosphatase domain. It may have a coiled-coil domain, but it is much weaker compared with other myotubularins using coiled-coil detection programs [http://www.ch.embnet.org/software/COILS_form.html COILS] and [http://paircoil2.csail.mit.edu/paircoil2.html PAIRCOIL2]. While most active myotubularins dimerize with inactive homologs through the coiled coil domain, no such inactive partner has been described for MTMR14, which may explain the weak coiled-coil score.
 Choanoflagellate Monosiga has a predicted transmembrane region (see [http://phosphatome.net/3.0/database/gene/uid/MbreP022 database]).
@@ Line 20: / Line 20: @@
 MTMR14 has also been shown to be involved in the regulation of autophagy <cite>Vergne10, Gibbs10</cite>.
-Drosophila MTMR14, EDTP (Egg-Derived Tyrosine Phosphatase) has roles in oogenesis, embryogenesis <cite>Yamaguchi</cite>, and muscle aging, and its expression is induced along with several other autophagy genes during starvation <cite>Erdi</cite>. Another insect homolog, from Sarcophaga peregrina, showed tyrosine phosphatase activity in vitro and was degraded by cathepsin L during embyrogenesis <cite>Yamaguchi99<cite>
+Drosophila MTMR14, EDTP (Egg-Derived Tyrosine Phosphatase) has roles in oogenesis, embryogenesis <cite>Yamaguchi</cite>, and muscle aging, and its expression is induced along with several other autophagy genes during starvation <cite>Erdi</cite>. Another insect homolog, from Sarcophaga peregrina, showed tyrosine phosphatase activity in vitro and was degraded by cathepsin L during embyrogenesis <cite>Yamaguchi99</cite>
 ===References===

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 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]:  [[Phosphatase_Family_Myotubularin|Family Myotubularin]]: [[Phosphatase_Subfamily_MTMR14|Subfamily MTMR14]]
-MTMR14 is an active phosphatase found in most holozoan and slime molds. Its putative substrates are phosphatidylinositol bisphophosphates PtdIns(3,5)P2 and PtdIns (3,4)P2.
+MTMR14 is an lipid phosphatase though to act on phosphatidylinositol bisphophosphates PtdIns(3,5)P2 and PtdIns (3,4)P2.
 ===Evolution===
@@ Line 9: / Line 9: @@
 ===Domain Structure===
-MTMR14 in eumetazoan has a conserved domain combination: a PH/GRAM domain and an active phosphatase domain. It may have a coiled-coil domain, but it is much weaker compared with other myotubularins using coiled-coil detection programs [http://www.ch.embnet.org/software/COILS_form.html COILS] and [http://paircoil2.csail.mit.edu/paircoil2.html PAIRCOIL2].
+MTMR14 in eumetazoa has a conserved domain combination: a PH/GRAM domain and an active phosphatase domain. It may have a coiled-coil domain, but it is much weaker compared with other myotubularins using coiled-coil detection programs [http://www.ch.embnet.org/software/COILS_form.html COILS] and [http://paircoil2.csail.mit.edu/paircoil2.html PAIRCOIL2].
 Choanoflagellate Monosiga has a predicted transmembrane region (see [http://phosphatome.net/3.0/database/gene/uid/MbreP022 database]).
@@ Line 19: / Line 19: @@
 MTMR14 has also been shown to be involved in the regulation of autophagy <cite>Vergne10, Gibbs10</cite>.
 ===References===
 <biblio>
 #tocsh06 pmid=17008356
 #shen09 pmid=19465920
 #Vergne10 pmid=19590496
 #Gibbs10 pmid=20595810
 </biblio>

@@ Line 6: / Line 6: @@
 ===Evolution===
-MTMR14 is found in most metazoan except nematodes. It is also found in choanoflagellates and cellular slime molds, but is absent from almost all the fungi. The result is based on BLAST nr database.
+MTMR14 is found in most metazoa except nematodes, and in scattered protists.
 ===Domain Structure===

@@ Line 11: / Line 11: @@
 MTMR14 in eumetazoan has a conserved domain combination: a PH/GRAM domain and an active phosphatase domain. It may have a coiled-coil domain, but it is much weaker compared with other myotubularins using coiled-coil detection programs [http://www.ch.embnet.org/software/COILS_form.html COILS] and [http://paircoil2.csail.mit.edu/paircoil2.html PAIRCOIL2].
-Sponge MTMR14 has an additional protein kinase domain (see [http://phosphatome.net/3.0/database/gene/uid/AqueP029 database]); Choanoflagellate Monosiga has a predicted transmembrane region (see [http://phosphatome.net/3.0/database/gene/uid/MbreP022 database]).
+Choanoflagellate Monosiga has a predicted transmembrane region (see [http://phosphatome.net/3.0/database/gene/uid/MbreP022 database]).
 ===Catalytic activity and functions===

@@ Line 1: / Line 1: @@
 __NOTOC__
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]:  [[Phosphatase_Family_Myotubularin|Family Myotubularin]]: [[Phosphatase_Subfamily_MTMR14|Subfamily MTMR14]]
 MTMR14 is an active phosphatase found in most holozoan and slime molds. Its putative substrates are phosphatidylinositol bisphophosphates PtdIns(3,5)P2 and PtdIns (3,4)P2.
@@ Line 14: / Line 14: @@
 ===Catalytic activity and functions===
-MTMR14 may dephosphorylate PtdIns(3,5)P2 and PtdIns (3,4)P2.
+Human MTMR14 (JUMPY) dephosphorylates PtdIns(3,5)P2 and PtdIns (3,4)P2.
 It is highly expressed in skeleton muscle and exogenous GFP-MTMR14 localizes to the Golgi apparatus in vitro <cite>tocsh06</cite>. Mice deficient in MTMR14 show muscle weakness and fatigue. The mechanism model behind is deficiency in MTMR14 causes accumulation of its substrates, especially PtdIns(3,5)P2 and PtdIns (3,4)P2, which bind, and directly activate, the Ca2+ release channel (ryanodine receptor 1, RyR1) of the internal store - the sarcoplasmic reticulum, and the activation of RyR1 results in the spontaneous Ca2+ leakage from the sarcoplasmic reticulum <cite>shen09</cite>.

← Older revision		Revision as of 18:08, 31 December 2014
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	It is highly expressed in skeleton muscle and exogenous GFP-MTMR14 localizes to the Golgi apparatus in vitro <cite>tocsh06</cite>. Mice deficient in MTMR14 show muscle weakness and fatigue. The mechanism model behind is deficiency in MTMR14 causes accumulation of its substrates, especially PtdIns(3,5)P2 and PtdIns (3,4)P2, which bind, and directly activate, the Ca2+ release channel (ryanodine receptor 1, RyR1) of the internal store - the sarcoplasmic reticulum, and the activation of RyR1 results in the spontaneous Ca2+ leakage from the sarcoplasmic reticulum <cite>shen09</cite>.		It is highly expressed in skeleton muscle and exogenous GFP-MTMR14 localizes to the Golgi apparatus in vitro <cite>tocsh06</cite>. Mice deficient in MTMR14 show muscle weakness and fatigue. The mechanism model behind is deficiency in MTMR14 causes accumulation of its substrates, especially PtdIns(3,5)P2 and PtdIns (3,4)P2, which bind, and directly activate, the Ca2+ release channel (ryanodine receptor 1, RyR1) of the internal store - the sarcoplasmic reticulum, and the activation of RyR1 results in the spontaneous Ca2+ leakage from the sarcoplasmic reticulum <cite>shen09</cite>.
		+
		+	MTMR14 has also been shown to be involved in the regulation of autophagy <cite>Vergne10, Gibbs10</cite>.

	===References===		===References===