Difference between revisions of "Pseudophosphatases (obsolete)"
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=== Functions === | === Functions === | ||
| + | * Receptor PTPs. Most receptor PTPs have two tandem phosphatase domains. The 2nd phosphatase domain has no or negligible activity. The 2nd domain can interact with 1st domain in both intra- and intermolecular manners <cite>denHertog02</cite>. | ||
| − | === | + | === Controversial === |
| − | + | * PTPRN (IA-2) and PTPRN2. Human PTPRN and PTPRN2 have been proposed to be enzymatically inactive due to mutations at catalytic Cx5R motif and WPD motif <cite>Kharitidi13</cite>. However, PTPRN2 has been reported to be phosphatidylinositol phosphatase <cite>Caromile10</cite>. | |
=== References === | === References === | ||
<biblio> | <biblio> | ||
| + | #Caromile10 pmid=20097759 | ||
#denHertog02 pmid=12376545 | #denHertog02 pmid=12376545 | ||
| + | #Kharitidi13 pmid=24064037 | ||
</biblio> | </biblio> | ||
Revision as of 05:27, 10 March 2015
List of pseudophosphatases
To be added.
Functions
- Receptor PTPs. Most receptor PTPs have two tandem phosphatase domains. The 2nd phosphatase domain has no or negligible activity. The 2nd domain can interact with 1st domain in both intra- and intermolecular manners [1].
Controversial
- PTPRN (IA-2) and PTPRN2. Human PTPRN and PTPRN2 have been proposed to be enzymatically inactive due to mutations at catalytic Cx5R motif and WPD motif [2]. However, PTPRN2 has been reported to be phosphatidylinositol phosphatase [3].
References
- Blanchetot C, Tertoolen LG, Overvoorde J, and den Hertog J. Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases. J Biol Chem. 2002 Dec 6;277(49):47263-9. DOI:10.1074/jbc.M205810200 |
- Kharitidi D, Manteghi S, and Pause A. Pseudophosphatases: methods of analysis and physiological functions. Methods. 2014 Jan 15;65(2):207-18. DOI:10.1016/j.ymeth.2013.09.009 |
- Caromile LA, Oganesian A, Coats SA, Seifert RA, and Bowen-Pope DF. The neurosecretory vesicle protein phogrin functions as a phosphatidylinositol phosphatase to regulate insulin secretion. J Biol Chem. 2010 Apr 2;285(14):10487-96. DOI:10.1074/jbc.M109.066563 |
