| URN | urn:agi-ProtModification:inout-urn:agi-llid:5801:out-urn:agi-llid:5594::negative:dephosphorylation |
|---|---|
| References | 9 |
| Connectivity | 2 |
| Effect | negative |
| Mechanism | dephosphorylation |
| Original # of References | 9 |
| TextRef | info:pmid/19424502#abs:3 |
|---|---|
| PubYear | 2009 |
| MedlineTA | PLoS ONE |
| MedLine Reference | 19424502:2 |
| Sentence | PTP-SL is a major regulator of ERK2 activity. |
| TextRef | info:pmid/10066421#abs:5 |
|---|---|
| PubYear | 1999 |
| MedlineTA | Biochem Biophys Res Commun |
| MedLine Reference | 10066421:4 |
| Sentence | Here we report inactivation of the extracellular signal-regulated kinase (ERK) family Mitogen-activated protein kinase by PTPBR7. |
| TextMods | 86: 'MAPK ' -> 'Mitogen-activated protein kinase ' |
| Organ | Brain |
| TextRef | info:pmid/11493009#abs:3 |
|---|---|
| PubYear | 2001 |
| MedlineTA | J Mol Biol |
| MedLine Reference | 11493009:2 |
| Sentence | Specifically, the complex formation between PTP-SL and ERK2 involves an unusual interaction leading to the phosphorylation of PTP-SL by ERK2 at Thr253 and the inactivating dephosphorylation of ERK2 by PTP-SL. |
| TextRef | info:pmid/11856337#body:169 |
|---|---|
| PubYear | 2002 |
| MedlineTA | Eur J Biochem |
| MedLine Reference | 11856337:1168 |
| Sentence | PTP-SL dephosphorylates both ERK and p38 [19,78]. |
| CellType | Neurons |
| TextRef | info:pmid/10394362#body:189 |
|---|---|
| PubYear | 1999 |
| MedlineTA | Mol Cell |
| MedLine Reference | 10394362:1188 |
| Sentence | Interestingly, PTP-SL dephosphorylates and downregulates ERK in vitro and reduces ERK2 activity in transfected tissue culture cells ( [34]). |
| CellType | Epithelial Cells |
| TextRef | info:pmid/12754301#body:196 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Mol Cancer Res |
| MedLine Reference | 12754301:1195 |
| Sentence | In this respect, protein tyrosine phosphatase[varepsilon] is somewhat similar to PTP-SL, the transmembrane and cytosolic isoforms of which are able to dephosphorylate ERK2 (41). |
| TextMods | 17: 'PTP' -> 'protein tyrosine phosphatase' |
| TextRef | info:pmid/11579215#body:320 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Mol Endocrinol |
| MedLine Reference | 11579215:1319 |
| Sentence | Interestingly, other phosphotyrosine phosphatases, namely PTP-SL and striatum enriched phosphatase, were previously reported to directly interact and dephosphorylate ERK1/2 (39). |
| TextMods | 21: 'PTPs' -> 'phosphotyrosine phosphatases' |
| Organ | Corpus striatum |
| TextRef | info:pmid/11711538#body:165 |
|---|---|
| PubYear | 2002 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 11711538:1164 |
| Sentence | As shown, GST-PTP-SL dephosphorylated efficiently both ERK2 and p38alpha wild type, whereas the dephosphorylation of ERK2 D319N, ERK2 D160N, or p38alpha D316N mutations was impaired, indicating that the defective binding to these mitogen-activated protein kinases hampers their dephosphorylation by PTP-SL. |
| TextMods | 230: 'MAP ' -> 'mitogen-activated protein ' |
| TextRef | info:pmid/15509801#body:284 |
|---|---|
| PubYear | 2004 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 15509801:1283 |
| Sentence | To determine whether Extracellular signal-regulated kinase1c is also resistant to phosphatases, we cotransfected COS7 cells with either green fluorescent protein-Extracellular signal-regulated kinase1c or green fluorescent protein-ERK1 together with increasing amounts of hemagglutinin tag-PTP-SL, a tyrosine phosphatase that was shown to bind and dephosphorylate ERK1 and ERK2 (27). |
| TextMods | 21: 'ERK' -> 'Extracellular signal-regulated kinase' 136: 'GFP' -> 'green fluorescent protein' 162: 'ERK' -> 'Extracellular signal-regulated kinase' 205: 'GFP' -> 'green fluorescent protein' 272: 'HA' -> 'hemagglutinin tag' |
| Tissue | Serum |