Phosphatase Family EYA - Revision history

Gerard at 22:33, 27 September 2018

2018-09-27T22:33:15Z

Gerard at 04:42, 9 May 2016

2016-05-09T04:42:17Z

Mark: /* Function */

2015-04-01T00:00:42Z

‎Function

Mark at 23:59, 31 March 2015

2015-03-31T23:59:33Z

Gerard: /* Related kinase */

2015-03-21T21:05:43Z

‎Related kinase

Gerard at 21:05, 21 March 2015

2015-03-21T21:05:18Z

Mark at 03:57, 1 January 2015

2015-01-01T03:57:33Z

Mark at 03:56, 1 January 2015

2015-01-01T03:56:43Z

Mark: /* Function */

2015-01-01T03:51:32Z

‎Function

Mark: /* Domain */

2015-01-01T03:51:09Z

‎Domain

@@ Line 2: / Line 2: @@
 [[Phosphatase classification|Phosphatase Classification]]:  [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_EYA|Family EYA]]
-EYA (EYes Absent) was first identified in Drosophila as a gene required for eye development. There are four members in human, and a single copy in most invetebrates. All EYAs belong to [[Phosphatase_Subfamily_EYA|EYA subfamily]], the single subfamily of EYA family.
+EYA (EYes Absent) was first identified in Drosophila as a gene required for eye development. There are four members in human, and a single copy in most invetebrates. This family contains a single subfamily, also named [[Phosphatase_Subfamily_EYA|EYA]].
 === Evolution ===
-EYA can be found in animal and choanoflagellates, plants and Phytophthora. But in plants and Phytophthora, while the phosphatase domain is conserved and complete, the N-terminal transcriptional factor domain is very short and may be even not a domain. (Note: in some non-model animals, no N-terminal region was found, either.) Interestingly, EYA is only found in Phytophthora genus rather than other genera in heterokonts.
+EYA is found in animals and choanoflagellates, and also plants and Phytophthora. The N-terminal transcription factor domain is absent or short and degraded in both plants and Phytophthora, suggesting it may have distinct functions. EYA is only found in Phytophthora genus rather than other genera in heterokonts.
-The catalytic motif sequences varies. From Monosiga to human, most EYAs have the canonical catalytic motif sequence DLDET, except Hydra (DLDDV) and nematodes. In particular, all nematodes except Trichinella spiralis have neither conserved nor canonical sequence motif (DIDDI, DLEDV, EMEDV). In plants, the catalytic motif sequence is conserved as DMDET, and in phytophora, that is DLDET again.
+The catalytic motif sequences varies. From Monosiga to human, most EYAs have the canonical catalytic motif sequence DLDET, except Hydra (DLDDV) and nematodes. In particular, all nematodes except Trichinella spiralis have neither conserved nor canonical sequence motif (DIDDI, DLEDV, EMEDV). In plants, the catalytic motif sequence is conserved as DMDET, and in Phytophora, that is DLDET again.
-Human (and most vertebrates) has four copies of EYAs; Sea urchin has three copies; Non-chordates such as fruit fly and ''C elegans'' have single copy per genome.
+Human, and most vertebrates, have four copies of EYAs; Sea urchin has three copies; Most invertebrates such as fruit fly and ''C elegans'' have a single copy.
-=== Domain ===
+=== Domain Structure===
-EYA has two regions corresponding to its two main function. The N-terminal region is transcriptional factor domain, and the C-terminal region is a HAD-fold phosphatase domain (known as ED) <cite>tootle04</cite>.
+EYA has two regions corresponding to its two main function. The N-terminal region, in animals and choanoflagellates, is transcriptional factor domain, and the C-terminal region is a HAD-fold phosphatase domain (known as ED) <cite>tootle04</cite>.
 === Function ===
 Putative substrates are myelin basic protein, RNA pol II, MAPK, and EYA itself (see Review <cite>Jmec07</cite>).
-EYA is involved in apoptosis by dephosphorylating Y142 of the histone variant H2AX in mouse <cite>Cook09</cite>, and through direct transcriptional activation of egl-1 in C. elegans <cite>Hirose10</cite>. However, the molecular mechanism of how EYA involved in apoptosis may be not conserved, because no Y142 is found in C. elegans (Note: The existence of H2AX in C. elegans is plausible. No H2AX has been identified in C. elegans. Even though some researchers suggest CENP-A function as H2AX, the protein has no Y142.)
+EYA is involved in apoptosis by dephosphorylating Y142 of the histone variant H2AX in mouse <cite>Cook09</cite>, and through direct transcriptional activation of egl-1 in C. elegans <cite>Hirose10</cite>. The existence of H2AX in C. elegans is uncertain - some have suggested CENP-A to be the functional analog, but it does not have an equivalent to Y142.
-Eya1 cooperates with the DNA-binding protein Six1 to promote gene induction in response to Shh and that Eya1/Six1 together regulate Gli transcriptional activators in normal hindbrain and Shh-dependent hindbrain tumor <cite>Eisner15</cite>.
+Eya1 cooperates with the DNA-binding protein Six1 to promote gene expression in response to Shh. Eya1/Six1 together regulate Gli transcriptional activators in normal hindbrain and Shh-dependent hindbrain tumors <cite>Eisner15</cite>.
 === Related kinase ===
@@ Line 25: / Line 25: @@
 === Correlated presence/absence of EYA and Y142 ===
-The presence/absence of EYA well correlates that of Y142. The Y142 is conserved from Nematostella to human with the exception of nematodes. Surprisingly, Phytophthora also have Y142, though most of the bikonts (plants + heterokonts + alveolates + excavates) do not have Y142. This implies 1) the H2AX Y142 is a real substrate of EYA, 2) EYA has other functions.
+The presence/absence of EYA well correlates that of Y142. The Y142 is conserved from Nematostella to human with the exception of nematodes. Surprisingly, Phytophthora also has Y142, though most of the bikonts (plants + heterokonts + alveolates + excavates) do not. The co-ordinated loss of Y142 and Eya function suggests that H2AX dephosphorylation is a major function of Eya
 === Reference ===

@@ Line 2: / Line 2: @@
 [[Phosphatase classification|Phosphatase Classification]]:  [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_EYA|Family EYA]]
-EYA (comes from eyes absent) was first identified in Drosophila as a gene required for eye development. There four copies in human, and a single copy in most of the invetebrates. All EYAs belong to [[Phosphatase_Subfamily_EYA|EYA subfamily]], the single subfamily of EYA family.
+EYA (EYes Absent) was first identified in Drosophila as a gene required for eye development. There are four members in human, and a single copy in most invetebrates. All EYAs belong to [[Phosphatase_Subfamily_EYA|EYA subfamily]], the single subfamily of EYA family.
 === Evolution ===
 EYA can be found in animal and choanoflagellates, plants and Phytophthora. But in plants and Phytophthora, while the phosphatase domain is conserved and complete, the N-terminal transcriptional factor domain is very short and may be even not a domain. (Note: in some non-model animals, no N-terminal region was found, either.) Interestingly, EYA is only found in Phytophthora genus rather than other genera in heterokonts.
-The catalytic motif sequences varies. From Monosiga to human, most of the EYAs have canonical catalytic motif sequence DLDET, except Hydra (DLDDV) and nematodes. In particular, all nematodes except Trichinella spiralis have neither conserved nor canonical sequence motif (DIDDI, DLEDV, EMEDV). In plants, the catalytic motif sequence is conserved as DMDET, and in phytophora, that is DLDET again.
+The catalytic motif sequences varies. From Monosiga to human, most EYAs have the canonical catalytic motif sequence DLDET, except Hydra (DLDDV) and nematodes. In particular, all nematodes except Trichinella spiralis have neither conserved nor canonical sequence motif (DIDDI, DLEDV, EMEDV). In plants, the catalytic motif sequence is conserved as DMDET, and in phytophora, that is DLDET again.
 Human (and most vertebrates) has four copies of EYAs; Sea urchin has three copies; Non-chordates such as fruit fly and ''C elegans'' have single copy per genome.

@@ Line 19: / Line 19: @@
 EYA is involved in apoptosis by dephosphorylating Y142 of the histone variant H2AX in mouse <cite>Cook09</cite>, and through direct transcriptional activation of egl-1 in C. elegans <cite>Hirose10</cite>. However, the molecular mechanism of how EYA involved in apoptosis may be not conserved, because no Y142 is found in C. elegans (Note: The existence of H2AX in C. elegans is plausible. No H2AX has been identified in C. elegans. Even though some researchers suggest CENP-A function as H2AX, the protein has no Y142.)
-<cite>Eisner15</cite>.
+Eya1 cooperates with the DNA-binding protein Six1 to promote gene induction in response to Shh and that Eya1/Six1 together regulate Gli transcriptional activators in normal hindbrain and Shh-dependent hindbrain tumor <cite>Eisner15</cite>.
 === Related kinase ===

@@ Line 18: / Line 18: @@
 EYA is involved in apoptosis by dephosphorylating Y142 of the histone variant H2AX in mouse <cite>Cook09</cite>, and through direct transcriptional activation of egl-1 in C. elegans <cite>Hirose10</cite>. However, the molecular mechanism of how EYA involved in apoptosis may be not conserved, because no Y142 is found in C. elegans (Note: The existence of H2AX in C. elegans is plausible. No H2AX has been identified in C. elegans. Even though some researchers suggest CENP-A function as H2AX, the protein has no Y142.)
 === Related kinase ===
@@ Line 27: / Line 29: @@
 === Reference ===
 <biblio>
 #tootle04 pmid=14628053
 #Jmec07 pmid=17341163

@@ Line 20: / Line 20: @@
 === Related kinase ===
-WSTF: WSTF is the kinase of H2AX Y142 <cite>Xiao09</cite>.
+WSTF phosphorylates H2AX on Y142 <cite>Xiao09</cite>.
-−
 === Correlated presence/absence of EYA and Y142 ===

@@ Line 14: / Line 14: @@
 === Function ===
-EYA has two regions corresponding to its two main function. The N-terminal region is transcriptional factor domain, and the C-terminal region is a phosphatase domain of HAD fold (known as ED). The substrate(s) of phosphatase domain is not totally clear. Putative substrates are myelin basic protein, RNA pol II, MAPK, and EYA itself (see Review <cite>Jmec07</cite>).
+EYA has two regions corresponding to its two main function. The N-terminal region is transcriptional factor domain, and the C-terminal region is a phosphatase domain of HAD fold (known as ED) <cite>tootle04</cite>. Putative substrates are myelin basic protein, RNA pol II, MAPK, and EYA itself (see Review <cite>Jmec07</cite>).
 Recently, Cook et al. showed EYA involved in apoptosis by dephosphorylating H2AX Y142 in mouse <cite>Cook09</cite>, and Hirose showed EYA involved in apoptosis through direct transcriptional activation of egl-1 in C. elegans <cite>Hirose10</cite>. However, the molecular mechanism of how EYA involved in apoptosis may be not conserved, because no Y142 is found in C. elegans (Note: The existence of H2AX in C. elegans is plausible. No H2AX has been identified in C. elegans. Even though some researchers suggest CENP-A function as H2AX, the protein has no Y142.)