Phosphatase Subfamily Auxilin - Revision history

Gerard: /* Domain Structure */

2025-03-14T00:55:42Z

‎Domain Structure

Gerard: /* Evolution */

2025-03-14T00:55:03Z

‎Evolution

Mark: /* Evolution */

2015-06-29T17:50:24Z

‎Evolution

Mark: /* Domain Structure */

2015-06-25T20:44:14Z

‎Domain Structure

Gerard at 06:51, 28 December 2014

2014-12-28T06:51:24Z

Gerard at 06:49, 28 December 2014

2014-12-28T06:49:06Z

Gerard: /* Functions */

2014-12-28T06:31:24Z

‎Functions

Gerard at 06:26, 28 December 2014

2014-12-28T06:26:13Z

Gerard at 06:25, 28 December 2014

2014-12-28T06:25:59Z

Gerard: Created page with "NOTOC Phosphatase Classification: Superfamily CC1: Family PTEN: Phosphatase_Su..."

2014-12-28T05:47:46Z

Created page with "__NOTOC__ Phosphatase Classification: Superfamily CC1: Family PTEN: Phosphatase_Su..."

New page

__NOTOC__
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTEN|Family PTEN]]: [[Phosphatase_Subfamily_Auxilin|Subfamily Auxilin]]

Header

===Evolution===

===Domain Structure===

===Functions===

===References===
<biblio>
#Hafizi pmid=20678486
#Koh pmid=23401856
</biblio>

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 ===Domain Structure===
-Most auxillins are 1000-1500 AA long, with an N-terminal GAK kinase domain, a PTEN-like phosphatase domain in the middle, and a DnaJ domain at the very C-terminus. One of the two human homologs, DNAJC6/Auxillin-1 has lost the kinase domain.
+Most auxillins are 1000-1500 AA long, with an N-terminal GAK kinase domain, a PTEN-like phosphatase domain in the middle, and a DnaJ domain at the very C-terminus. One of the two human homologs, DNAJC6/Auxillin-1 has lost the kinase domain, and the C. elegans homolog has lost all but the kinase domain (though other nematodes have a more complete gene).
 ===Functions===

@@ Line 5: / Line 5: @@
 ===Evolution===
-Auxilins are metazoan-specific, and lost from nematodes. Human has two members: auxilin and DNAJC6, which emerged by gene duplication in jawed vertebrates. The DNAJ domain appears to be much older and has orthologs in Arabidopsis (JAC1) and yeast (Swa2) that are also involved in clathrin uncoating, but lack phosphatase and kinase domains.
+Auxilins are metazoan-specific. Human has two members: auxilin and DNAJC6, which emerged by gene duplication in jawed vertebrates. The DNAJ domain appears to be much older and has orthologs in Arabidopsis (JAC1) and yeast (Swa2) that are also involved in clathrin uncoating, but lack phosphatase and kinase domains.
 ===Domain Structure===

@@ Line 5: / Line 5: @@
 ===Evolution===
-Auxillins are metazoan-specific, and lost from nematodes. The DNAJ domain appears to be much older and has orthologs in Arabidopsis (JAC1) and yeast (Swa2) that are also involved in clathrin uncoating, but lack phosphatase and kinase domains
+Auxilins are metazoan-specific, and lost from nematodes. Human has two members: auxilin and DNAJC6, which emerged by gene duplication in jawed vertebrates. The DNAJ domain appears to be much older and has orthologs in Arabidopsis (JAC1) and yeast (Swa2) that are also involved in clathrin uncoating, but lack phosphatase and kinase domains.
 ===Domain Structure===

@@ Line 8: / Line 8: @@
 ===Domain Structure===
-Most auxillins are 1000-1500 AA long, with an N-terminal GAK kinase domain, a PTEN-like phosphatase domain in the middle, and a DnaJ domain at the very C-terminus. One of the two human homologs, DNAJC6/Auxillin-1 has lost the kinase domain
+Most auxillins are 1000-1500 AA long, with an N-terminal GAK kinase domain, a PTEN-like phosphatase domain in the middle, and a DnaJ domain at the very C-terminus. One of the two human homologs, DNAJC6/Auxillin-1 has lost the kinase domain.
 ===Functions===

@@ Line 5: / Line 5: @@
 ===Evolution===
-Auxillins are metazoan-specific, and lost from nematodes.
+Auxillins are metazoan-specific, and lost from nematodes. The DNAJ domain appears to be much older and has orthologs in Arabidopsis (JAC1) and yeast (Swa2) that are also involved in clathrin uncoating, but lack phosphatase and kinase domains
 ===Domain Structure===
@@ Line 24: / Line 24: @@
 #Scheele pmid=11470803
 #Lee pmid=16895969
 </biblio>

@@ Line 2: / Line 2: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTEN|Family PTEN]]: [[Phosphatase_Subfamily_Auxilin|Subfamily Auxilin]]
-Header
+Auxillins are pseudophosphatases and kinases that bind phospholipids and are involved in clathrin-coated vesicle function. Human forms are associated with Parkinson's disease.
 ===Evolution===

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 Human DNAJC6 is only expressed in neuronal tissues, but GAK is widespread, and generally expressed higher in non-neuronal tissue. GAK and DNAJC6 bind clathrin heavy chain and are found in and required for the function of clathrin-associated vesicles, particularly by interacting with Hsc70 in uncoating of the vesicles <cite>Scheele </cite>. GAK also binds AP1 and is required for endosomal sorting <cite>Kametaka </cite>. GAK can also localize to the nucleus and is required in a clathrin-dependent manner for mitosis <cite>Shimizu</cite>.
-Little is known about the phosphatase or kinase activities of auxilins, though one report shows that GAK phosphorylates and activates the PP2A complex <cite>Naito</cite>. The phosphatase domains of both are predicted to be inactive (HCx5R changed to HCx5A in both), though the human GAK phosphatase domain has been reported to bind phospholipids, which are also involved in clathrin-coated vesicles <cite>Lee</cite>.
+Little is known about the phosphatase or kinase activities of auxilins, though one report shows that GAK phosphorylates and activates the PP2A complex <cite>Naito</cite>. The phosphatase domains of both are predicted to be inactive (HCx5R changed to HCx5A in both), and both GAK and DNAJC6 phosphatase domains have been shown to bind phospholipids, which are also involved in clathrin-coated vesicles <cite>Lee, Kalli</cite>.
 ===References===

@@ Line 11: / Line 11: @@
 ===Functions===
-Human GAK is known as Cyclin G-Associated Kinase, and associated with Cyclin G and CDK5 <cite>Kanaoka<cite>. Both GAK and DNAJC6 are genetically implicated in Parkinson's disease and GAK physically associates with the Parkinson's kinase, LRRK2.
+Human GAK is known as Cyclin G-Associated Kinase, and associated with Cyclin G and CDK5 <cite>Kanaoka</cite>. Both GAK and DNAJC6 are genetically implicated in Parkinson's disease and GAK physically associates with the Parkinson's kinase, LRRK2.
 Human DNAJC6 is only expressed in neuronal tissues, but GAK is widespread, and generally expressed higher in non-neuronal tissue. GAK and DNAJC6 bind clathrin heavy chain and are found in and required for the function of clathrin-associated vesicles, particularly by interacting with Hsc70 in uncoating of the vesicles <cite>Scheele </cite>. GAK also binds AP1 and is required for endosomal sorting <cite>Kametaka </cite>. GAK can also localize to the nucleus and is required in a clathrin-dependent manner for mitosis <cite>Shimizu</cite>.