Difference between revisions of "Pseudophosphatases (obsolete)"
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* [[Phosphatase_Subfamily_PTPRG|Subfamily PTPRK]]: PTPRK, PTPRM, PTPRT and PTPRU | * [[Phosphatase_Subfamily_PTPRG|Subfamily PTPRK]]: PTPRK, PTPRM, PTPRT and PTPRU | ||
| − | + | === [[Phosphatase_Subfamily_PTPN23|PTPN23 subfamily]] === | |
The subfamily has a single member in human, PTPN23 (HD-PTP). Its catalytic activity is plausible. It has been reported to be catalytically inactive, - no phosphatase activity toward tyrosine or lipid. It was proposed that serine at position 1452 within Cx5R catalytic motif caused the inactivity. Replacing serine with alanine, which is found in catalytically active PTPs, can restore the phosphatase activity <cite>Gingras09</cite>. However, another study found SRC, E-cadherin, and beta-catenin are direct substrates of PTPN23 <cite>Lin11</cite>. But, yet another study showed that PTPN23 did not modulate the levels of Src phosphorylation both in vitro and in vivo <cite>Mariotti09</cite>. | The subfamily has a single member in human, PTPN23 (HD-PTP). Its catalytic activity is plausible. It has been reported to be catalytically inactive, - no phosphatase activity toward tyrosine or lipid. It was proposed that serine at position 1452 within Cx5R catalytic motif caused the inactivity. Replacing serine with alanine, which is found in catalytically active PTPs, can restore the phosphatase activity <cite>Gingras09</cite>. However, another study found SRC, E-cadherin, and beta-catenin are direct substrates of PTPN23 <cite>Lin11</cite>. But, yet another study showed that PTPN23 did not modulate the levels of Src phosphorylation both in vitro and in vivo <cite>Mariotti09</cite>. | ||
Revision as of 00:34, 2 October 2015
Contents
Human pseudophosphatases
Second phosphatase domain (D2) in 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, therefore regulating RPTP stability, specificity, and dimerization [1, 2].
These phosphatases include:
- Subfamily PTPRA: PTPRA and PTPRE
- Subfamily PTPRC: PTPRC
- Subfamily PTPRD: PTPRD, PTPRF and PTPRS
- Subfamily PTPRG: PTPRG and PTPRZ1
- Subfamily PTPRK: PTPRK, PTPRM, PTPRT and PTPRU
PTPN23 subfamily
The subfamily has a single member in human, PTPN23 (HD-PTP). Its catalytic activity is plausible. It has been reported to be catalytically inactive, - no phosphatase activity toward tyrosine or lipid. It was proposed that serine at position 1452 within Cx5R catalytic motif caused the inactivity. Replacing serine with alanine, which is found in catalytically active PTPs, can restore the phosphatase activity [3]. However, another study found SRC, E-cadherin, and beta-catenin are direct substrates of PTPN23 [4]. But, yet another study showed that PTPN23 did not modulate the levels of Src phosphorylation both in vitro and in vivo [5].
Auxilin subfamily
There are two members of auxilin subfamily in human, GAK and DNAJC6. Both GAK and DNAJC6 phosphatase domains have been shown to bind phospholipids [6, 7]. The phosphatase domains of both are predicted to be inactive due to arginine in catalytic motif Cx5R is replaced by alanine.
References
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- Error fetching PMID 12376545:
- Error fetching PMID 19167335:
- Error fetching PMID 19340315:
- Error fetching PMID 21724833:
- Error fetching PMID 18762272:
- Error fetching PMID 16895969:
- Error fetching PMID 23823232:
- Error fetching PMID 20097759:
- Error fetching PMID 24064037:
