Phosphatase Subfamily Synaptojanin - Revision history

Gerard: /* Domain */

2016-12-21T23:31:17Z

‎Domain

Gerard at 23:27, 21 December 2016

2016-12-21T23:27:18Z

Gerard: /* Evolution */

2016-12-21T23:25:51Z

‎Evolution

Gerard: /* Domain */

2016-12-21T23:25:33Z

‎Domain

Mark: /* Domain */

2015-04-29T17:05:41Z

‎Domain

Mark at 17:05, 29 April 2015

2015-04-29T17:05:17Z

Mark: /* Evolution */

2015-04-18T16:47:40Z

‎Evolution

Mark: /* Human SYNJ2 */

2015-04-18T16:41:11Z

‎Human SYNJ2

Mark: /* References */

2015-04-18T16:35:48Z

‎References

Mark at 14:50, 18 April 2015

2015-04-18T14:50:22Z

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 === Domain ===
-Synaptojanin has two domains, a Sac phosphatase domain and a 5-phosphatase domain. Both domains are active, which dephosphorylate 3' and 5' positions of phosphatidylinositol(4,5)bisphosphate (PI(4,5)P2), respectively. This domain combination enables synaptojanin to hydrolyse PI(4,5)P2 to PI without producing another signal, PI4P <cite> Hughes01 </cite>. The Sac phosphatase domain also mediates the targeting of synaptojanin to synapses <cite>Dong15</cite>.
+Synaptojanin has two domains, a Sac phosphatase domain and a 5-phosphatase domain. Both domains are active, which dephosphorylate 3' and 5' positions of phosphatidylinositol(4,5)bisphosphate (PI(4,5)P2), respectively. This domain combination enables synaptojanin to hydrolyse PI(4,5)P2 to PI without producing another signal, PI4P <cite> Hughes01 </cite>. The Sac phosphatase domain also mediates the targeting of synaptojanin to synapses <cite>Dong15</cite>. Synaptojanin also has a DUF1866 domain just following the phosphatase domain. This is only found in these phosphatases but is related to other domains, including the RRM RNA-biding domain (see http://pfam.xfam.org/family/PF08952.6#tabview=tab2).
 Synaptojanin also has a proline-rich region at C-terminal tail <cite> Zucconi01 </cite>., which binds to SH3 or WW domains of other proteins (e.g. endophilin and amphiphysin,  EEN and Abi-1).  The SH3 domains of different proteins bind to different sites of the proline-rich region <cite>Cestra99, So00</cite>.

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 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]:  [[Phosphatase_Family_Sac|Family Sac]]: [[Phosphatase_Subfamily_Synaptojanin|Subfamily Synaptojanin]]
-Synaptojanin is a PtdIns(3,5)P2 phosphatase in the endocytic pathway. It has two phosphatase domains dephosphorylate 3-position and 5-position of PtdIns(3,5)P2, respectively. It is found throughout eukaryotes except excavate and some chromalveolate. Human has two members (SYNJ1/INPP5G and SYNJ2/INPP5H) which originated from a duplication event in tetrapods.
+Synaptojanin is a PtdIns(3,5)P2 phosphatase in the endocytic pathway. It has two phosphatase domains that dephosphorylate both the 3' and 5' phosphates of PtdIns(3,5)P2.
 === Evolution ===
-Synaptojanin is found throughout eukaryotes except excavate and some chromalveolates. Human has two members (SYNJ1/INPP5G and SYNJ2/INPP5H) which originated from a duplication event in tetrapods  ([http://resdev.gene.com/gOrtholog/view/cluster/MC0001117/overview internal data of gOrtholog database]).
+Synaptojanin is found throughout eukaryotes except excavates and some chromalveolates. Human has two members (SYNJ1/INPP5G and SYNJ2/INPP5H) which originated from a duplication event in tetrapods  ([http://resdev.gene.com/gOrtholog/view/cluster/MC0001117/overview internal data of gOrtholog database]).
 === Domain ===

@@ Line 5: / Line 5: @@
 === Evolution ===
-Synaptojanin is found throughout eukaryotes except excavate and some chromalveolate. Human has two members (SYNJ1/INPP5G and SYNJ2/INPP5H) which originated from a duplication event in tetrapods  ([http://resdev.gene.com/gOrtholog/view/cluster/MC0001117/overview internal data of gOrtholog database]).
+Synaptojanin is found throughout eukaryotes except excavate and some chromalveolates. Human has two members (SYNJ1/INPP5G and SYNJ2/INPP5H) which originated from a duplication event in tetrapods  ([http://resdev.gene.com/gOrtholog/view/cluster/MC0001117/overview internal data of gOrtholog database]).
 === Domain ===

@@ Line 8: / Line 8: @@
 === Domain ===
-Synaptojanin has two domains, a Sac phosphatase domain and a 5-phosphatase domain. Both domains are active, which dephosphorylate 3-position and 5-position of phosphatidylinositol(4,5)bisphosphat e (PI(4,5)P2), respectively. This domain combination enables synaptojanin to hydrolyse PI(4,5)P2 to PI without producing another signal, PI4P <cite> Hughes01 </cite>. The Sac phosphatase domain also mediates the targeting of synaptojanin to synapses <cite>Dong15</cite>.
+Synaptojanin has two domains, a Sac phosphatase domain and a 5-phosphatase domain. Both domains are active, which dephosphorylate 3' and 5' positions of phosphatidylinositol(4,5)bisphosphate (PI(4,5)P2), respectively. This domain combination enables synaptojanin to hydrolyse PI(4,5)P2 to PI without producing another signal, PI4P <cite> Hughes01 </cite>. The Sac phosphatase domain also mediates the targeting of synaptojanin to synapses <cite>Dong15</cite>.
 Synaptojanin also has a proline-rich region at C-terminal tail <cite> Zucconi01 </cite>., which binds to SH3 or WW domains of other proteins (e.g. endophilin and amphiphysin,  EEN and Abi-1).  The SH3 domains of different proteins bind to different sites of the proline-rich region <cite>Cestra99, So00</cite>.

@@ Line 8: / Line 8: @@
 === Domain ===
-Synaptojanin has two domains, a Sac phosphatase domain and a 5-phosphatase domain. Both domains are active, which dephosphorylate 3-position and 5-position of phosphatidylinositol(4,5)bisphosphat e (PI(4,5)P2), respectively. This domain combination enables synaptojanin to hydrolyse PI(4,5)P2 to PI without producing another signal, PI4P <cite> Hughes01 </cite>. The Sac phosphatase domain also targets synaptojanin to synapses <cite>Dong15</cite>.
+Synaptojanin has two domains, a Sac phosphatase domain and a 5-phosphatase domain. Both domains are active, which dephosphorylate 3-position and 5-position of phosphatidylinositol(4,5)bisphosphat e (PI(4,5)P2), respectively. This domain combination enables synaptojanin to hydrolyse PI(4,5)P2 to PI without producing another signal, PI4P <cite> Hughes01 </cite>. The Sac phosphatase domain also mediates the targeting of synaptojanin to synapses <cite>Dong15</cite>.
 Synaptojanin also has a proline-rich region at C-terminal tail <cite> Zucconi01 </cite>., which binds to SH3 or WW domains of other proteins (e.g. endophilin and amphiphysin,  EEN and Abi-1).  The SH3 domains of different proteins bind to different sites of the proline-rich region <cite>Cestra99, So00</cite>.
 === Function ===

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 === Domain ===
-Synaptojanin has two domains, a CC1-fold phosphatase domain and a 5-phosphatase domain. Both domains are active, which dephosphorylate 3-position and 5-position of phosphatidylinositol(4,5)bisphosphat e (PI(4,5)P2), respectively. This domain combination enables synaptojanin to hydrolyse PI(4,5)P2 to PI without producing another signal, PI4P <cite></cite>.
+Synaptojanin has two domains, a Sac phosphatase domain and a 5-phosphatase domain. Both domains are active, which dephosphorylate 3-position and 5-position of phosphatidylinositol(4,5)bisphosphat e (PI(4,5)P2), respectively. This domain combination enables synaptojanin to hydrolyse PI(4,5)P2 to PI without producing another signal, PI4P <cite> Hughes01 </cite>. The Sac phosphatase domain also targets synaptojanin to synapses <cite>Dong15</cite>.
 Synaptojanin also has a proline-rich region at C-terminal tail <cite> Zucconi01 </cite>., which binds to SH3 or WW domains of other proteins (e.g. endophilin and amphiphysin,  EEN and Abi-1).  The SH3 domains of different proteins bind to different sites of the proline-rich region <cite>Cestra99, So00</cite>.
 === Function ===
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 #Chuang04 pmid=15548694
 #Chuang12 pmid=23076136
 #Haffner97 pmid=9428629
 #Hughes01 pmid=11413010

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 SNYJ2 mRNA was first detected in neurons of the olfactory bulb, the cerebral cortex, the hippocampus, and the cerebellar cortex on early postnatal days <cite>Kudo99</cite>. According to [http://www.gtexportal.org/home/gene/SYNJ2 GTEx data], SYNJ2 is widely expressed in diverse tissues and most abundantly expressed in brain, especially in spinal cord.  In contrast, SYNJ1 is expressed in a relative low level in spinal cord compared with other parts of brain.
-SYNJ2 functions in endocytosis as well as SYNJ1. However, it is involved in clathrin-mediated receptor internalization, an early step of endocytosis; in contrast, SYNJ1 is involved in vesicle uncoating, a late step of endocytosis <cite>Rusk03</cite>. In fact, SYNJ2 have different though overlapping interacting partners. It interacts with GRB2, but not amphiphysin, both of which interact with SYNJ1. This is supported by the sequence differences of SYNJ1 and SYNJ2 in their proline-rich regions <cite> Nemoto97</cite>.
+SYNJ2 functions in endocytosis as well as SYNJ1. However, it is involved in clathrin-mediated receptor internalization, an early step of endocytosis; in contrast, SYNJ1 is involved in vesicle uncoating, a late step of endocytosis <cite>Rusk03</cite>.
-SYNJ2 regulates clathrin-mediated endocytosis as the effector of the small GTPase Rac <cite>Malecz00, Chuang04</cite>.
+SYNJ2 has at least three different isoforms, SYNJ2A, SYNJ2B1, SYNJ2B2. The isoforms have different though overlapping interacting partners.  This is supported by the sequence differences of SYNJ1 and different isoforms SYNJ2 in their proline-rich regions <cite> Nemoto97, Nemoto99, Nemoto01</cite>.
 SYNJ2 is phosphorylated and activated by Src through the phosphorylation of Tyr-490 in vitro <cite>Chuang12</cite>. Tyr-490 locates in the linker between two phosphatase domains.

@@ Line 55: / Line 55: @@
 #Micheva97 pmid=9341169
 #Nemoto97 pmid=9388224
 #Olgiati14 pmid=24816432
 #Picillo14 pmid=24532203