Phosphatase Subfamily EYA - Revision history

Gerard at 08:00, 25 July 2017

2017-07-25T08:00:34Z

Mark at 03:57, 1 January 2015

2015-01-01T03:57:47Z

Mark: Created page with "Phosphatase Classification: Fold HAD: Superfamily HAD: Phosphatase_Family_EYA|Family..."

2015-01-01T03:57:23Z

Created page with "Phosphatase Classification: Fold HAD: Superfamily HAD: Phosphatase_Family_EYA|Family..."

New page

[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_EYA|Family EYA]]: [[Phosphatase_Subfamily_EYA|EYA subfamily]]

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.

=== 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.

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.

=== Domain ===
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>.

=== 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) <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.)

== Related kinase ==
WSTF: WSTF is the kinase of H2AX Y142 <cite>Xiao09</cite>.

== 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.

== Reference ==
<biblio>
#tootle04 pmid=14628053
#Jmec07 pmid=17341163
#Cook09 pmid=19234442
#Hirose10 pmid=20713707
#Xiao09 pmid=19092802
</biblio>

← Older revision		Revision as of 03:57, 1 January 2015
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−	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_HAD\|Fold HAD]]: [[Phosphatase_Superfamily_HAD\|Superfamily HAD]]: [[Phosphatase_Family_EYA\|Family EYA]]: [[Phosphatase_Subfamily_EYA\|EYA ~~subfamily~~]]	+	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_HAD\|Fold HAD]]: [[Phosphatase_Superfamily_HAD\|Superfamily HAD]]: [[Phosphatase_Family_EYA\|Family EYA]]: [[Phosphatase_Subfamily_EYA\|Subfamily EYA]]

@@ Line 1: / Line 1: @@
 [[Phosphatase classification|Phosphatase Classification]]:  [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_EYA|Family EYA]]: [[Phosphatase_Subfamily_EYA|Subfamily EYA]]
+EYA (comes from eyes absent) was first identified in Drosophila as a gene required for eye development. There four members in human, and a single copy in most of the invertebrates. All EYAs belong to [[Phosphatase_Subfamily_EYA|EYA subfamily]], the single subfamily of EYA family.
-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.
 === 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, plants and Phytophthora. But in plants and Phytophthora, while the phosphatase domain is conserved and complete, the N-terminal transcription factor domain is very short and may be even not a domain. (in some non-model animals, no N-terminal region was found, either). EYA is only found in Phytophthora genus but not in other 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 of the EYAs have canonical catalytic motif sequence DLDET, except Hydra (DLDDV) and nematodes. 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.
 === Domain ===
-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>.
+EYA has two regions corresponding to its two main function. The N-terminal region is transcription factor domain, and the C-terminal region is a HAD-fold phosphatase domain (known as ED) <cite>tootle04</cite>.
 === 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) <cite>tootle04</cite>. Putative substrates are myelin basic protein, RNA pol II, MAPK, and EYA itself (see Review <cite>Jmec07</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.)