| URN | urn:agi-ProtModification:inout-urn:agi-llid:1848:out-urn:agi-llid:5595::negative:dephosphorylation |
|---|---|
| References | 9 |
| Connectivity | 2 |
| Effect | negative |
| Mechanism | dephosphorylation |
| Original # of References | 9 |
| TextRef | info:pmid/18771677#abs:2 |
|---|---|
| PubYear | 2008 |
| MedlineTA | Toxicol Appl Pharmacol |
| MedLine Reference | 18771677:1 |
| Sentence | When transiently overexpressed, MKP-3 dephosphorylates and inactivates extracellular signal regulated kinase (ERK) 1/2. |
| TextRef | info:pmid/19476641#abs:4 |
|---|---|
| PubYear | 2009 |
| MedlineTA | Mol Pain |
| MedLine Reference | 19476641:3 |
| Sentence | JWH015 (a Cannabinoid receptor type 2 agonist) increased MKP-1 and MKP-3 expression, which in turn reduced p-ERK1/2 in LPS-stimulated primary microglia. |
| TextMods | 10: 'CBR2 ' -> 'Cannabinoid receptor type 2 ' |
| CellType | Microglia |
| TextRef | info:pmid/11998972#abs:11 |
|---|---|
| PubYear | 2002 |
| MedlineTA | Basic Res Cardiol |
| MedLine Reference | 11998972:10 |
| Sentence | These results indicate that Ang II-induced apoptosis signaling in human endothelial cells is mediated via MKP-3-dependent dephosphorylation of ERK1/2, which in turn leads to the degradation of Bcl-2. |
| TextMods | 72: 'EC ' -> 'endothelial cells ' |
| CellType | Endothelial Cells |
| Organism | Homo sapiens |
| TextRef | info:pmid/12840032#abs:1 |
|---|---|
| PubYear | 2003 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 12840032:0 |
| Sentence | The mechanism of senescence-associated cytoplasmic induction of p-Erk1/2 (SA-p-Erk1/2) proteins in human diploid fibroblasts was investigated. p-Erk1/2 proteins were efficiently dephosphorylated in vitro by protein phosphatases 1 and 2A (PP1/2A) and MAPK phosphatase 3 (MKP3). |
| CellType | Fibroblasts |
| TextRef | info:pmid/11239467#body:71 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Mol Cell |
| MedLine Reference | 11239467:1070 |
| Sentence | When transiently overexpressed, MKP-3 dephosphorylates and inactivates extracellular signal regulated kinase (ERK) 1/2. |
| TextRef | info:pmid/11064451#body:106 |
|---|---|
| PubYear | 2000 |
| MedlineTA | Oncogene |
| MedLine Reference | 11064451:1105 |
| Sentence | Pyst1 has been shown to dephosphorylate both ERK1 and 2 but not JNK or p38 (Groom et al., 1996). |
| CellLineName | 293T |
| TextRef | info:pmid/20051628#body:241 |
|---|---|
| PubYear | 2010 |
| MedlineTA | J Clin Invest |
| MedLine Reference | 20051628:1240 |
| Sentence | The induced MKP-3 dephosphorylated p-ERK1/2 and therefore restrained the subsequent intensity of TCR signaling and, hence, cytokine production. |
| CellType | T-Lymphocytes |
| TextRef | info:pmid/19091959#body:80 |
|---|---|
| PubYear | 2009 |
| MedlineTA | Am J Physiol Cell Physiol |
| MedLine Reference | 19091959:1079 |
| Sentence | We show that incubation of aortic endothelial cells with Sphingosine-1-phosphate triggers rapid induction of MKP-3, which dephosphorylates ERK1/2. |
| TextMods | 34: 'EC ' -> 'endothelial cells ' 57: 'S1P ' -> 'Sphingosine-1-phosphate ' |
| CellType | Endothelial Cells |
| Organ | Aorta |
| TextRef | info:pmid/16135819#body:51 |
|---|---|
| PubYear | 2005 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 16135819:1050 |
| Sentence | The selective dephosphorylation of ERK1/2 by DUSP6/MKP-3 is accompanied by the formation of a stable complex between these two enzymes in which mitogen-activated protein kinase recognition and binding are mediated by a conserved motif within the amino-terminal noncatalytic domain of the phosphatase (13, 22). |
| TextMods | 144: 'MAPK ' -> 'mitogen-activated protein kinase ' |