| URN | urn:agi-ProtModification:inout-urn:agi-llid:1848:out-urn:agi-llid:5594::negative:dephosphorylation |
|---|---|
| References | 22 |
| Connectivity | 2 |
| Effect | negative |
| Mechanism | dephosphorylation |
| Original # of References | 22 |
| TextRef | info:pmid/11432864#abs:3 |
|---|---|
| PubYear | 2001 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 11432864:2 |
| Sentence | To gain insight into the mechanism of ERK2 inactivation by MKP3, we have carried out an analysis of the MKP3-catalyzed dephosphorylation of the phosphorylated ERK2. |
| 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/14690430#title:1 |
|---|---|
| PubYear | 2003 |
| MedLine Reference | 14690430:100 |
| Sentence | Intramolecular dephosphorylation of ERK by MKP3. |
| TextRef | info:pmid/16299265#body:286 |
|---|---|
| PubYear | 2006 |
| MedlineTA | Am J Physiol Heart Circ Physiol |
| MedLine Reference | 16299265:1285 |
| Sentence | The most specific of the three phosphatases is MKP-3, which mainly dephosphorylates ERK (23). |
| TextRef | info:pmid/15590690#body:248 |
|---|---|
| PubYear | 2005 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 15590690:1247 |
| Sentence | ERK was phosphorylated as MKP-3 became insoluble in a time-dependent manner. |
| CellType | Fibroblasts |
| TextRef | info:pmid/17046812#body:69 |
|---|---|
| PubYear | 2006 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 17046812:1068 |
| Sentence | The structural basis for the exquisite specificity of ERK2 dephosphorylation by MKP3 has not been elucidated. |
| 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/16195377#body:99 |
|---|---|
| PubYear | 2005 |
| MedlineTA | Proc Natl Acad Sci U S A |
| MedLine Reference | 16195377:1098 |
| Sentence | However, the first dephosphorylation of bisphosphorylated Erk2 by MKP3 is also predominantly on the tyrosine residue (8). |
| TextRef | info:pmid/14701731#body:182 |
|---|---|
| PubYear | 2004 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 14701731:1181 |
| Sentence | The result provides the direct evidence that Drosophila MKP-3 dephosphorylates Drosophila ERK in vivo. |
| TextMods | 45: 'DMKP-3 ' -> 'Drosophila MKP-3 ' 79: 'DERK ' -> 'Drosophila ERK ' |
| CellType | Photoreceptor Cells |
| Organ | Eye |
| TextRef | info:pmid/19897477#body:274 |
|---|---|
| PubYear | 2009 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 19897477:1273 |
| Sentence | As discussed earlier, this would decrease the efficiency of mitogen-activated protein kinase phosphatase3-dependent dephosphorylation of ERK. |
| TextMods | 60: 'MKP' -> 'mitogen-activated protein kinase phosphatase' |
| TextRef | info:pmid/11239467#body:318 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Mol Cell |
| MedLine Reference | 11239467:1317 |
| Sentence | The activated MKP-3 then catalyzes dephosphorylation of both phosphorylated T183 and Y185 in ERK2, leading to ERK2 inactivation View Within Article. |
| TextRef | info:pmid/15454482#body:200 |
|---|---|
| PubYear | 2005 |
| MedlineTA | Blood |
| MedLine Reference | 15454482:1199 |
| Sentence | They have, however, opposing functions: MEK2 phosphorylates, and thereby activates ERK2, whereas MKP3 dephosphorylates ERK2, taking it to an inactive state. |
| CellLineName | CEM |
| 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/11856337#body:67 |
|---|---|
| PubYear | 2002 |
| MedlineTA | Eur J Biochem |
| MedLine Reference | 11856337:1066 |
| Sentence | dual specificity protein phosphatases substrate studies indicate that MAPK phosphatase-3 (MKP-3) specifically dephosphorylates extracellular signal-regulated kinase (ERK) but not JNK or p38 [27,28]. |
| TextMods | 0: 'DSP ' -> 'dual specificity protein phosphatases ' |
| 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/16581800#body:67 |
|---|---|
| PubYear | 2006 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 16581800:1066 |
| Sentence | For example, MKP-3 dephosphorylates ERK, M3/6 dephosphorylates JNK, MKP-1 dephosphorylates JNK, ERK, and p38 (16), and MKP-8 (DUSP26) was recently shown to dephosphorylate p38 (43). |
| TextRef | info:pmid/14744999#body:84 |
|---|---|
| PubYear | 2004 |
| MedlineTA | J Cell Biol |
| MedLine Reference | 14744999:1083 |
| Sentence | ERK dephosphorylation by the phosphatase MKP3 was reported to follow a distributive, ordered mechanism in which the phosphotyrosine residue is dephosphorylated first and MpT dissociates from the enzyme (, where Mp stands for MpT) (Zhao and Zhang, 2001). |
| 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 ' |
| TextRef | info:pmid/16855216#body:265 |
|---|---|
| PubYear | 2007 |
| MedlineTA | Am J Physiol Cell Physiol |
| MedLine Reference | 16855216:1264 |
| Sentence | in cells that express oncogenic Ras, palytoxin can increase ERK activity by disrupting the action of mitogen-activated protein kinase phosphatase (mitogen-activated protein kinase phosphatase)-3, a dual-specificity protein phosphatase that specifically dephosphorylates and inactivates ERK.. |
| TextMods | 101: 'MAP ' -> 'mitogen-activated protein ' 147: 'MKP' -> 'mitogen-activated protein kinase phosphatase' |
| TextRef | info:pmid/14981092#body:49 |
|---|---|
| PubYear | 2004 |
| MedlineTA | J Cell Biol |
| MedLine Reference | 14981092:1048 |
| Sentence | Dual phosphorylation of mitogen-activated protein kinase on tyrosine and threonine by MEK occurs in the cytoplasm, and several nonspecific phosphoserine/phosphothreonine- and phosphotyrosine-specific phosphatases and a mitogen-activated protein kinase-specific phosphatase (MKP3) have been reported to dephosphorylate and inactivate p44/p42 mitogen-activated protein kinase/Erk (Camps et al., 1998; Keyse, 2000), effectively terminating the signal. |
| CellLineName | F9 |
| TextMods | 24: 'MAPK ' -> 'mitogen-activated protein kinase ' 219: 'MAPK' -> 'mitogen-activated protein kinase' 341: 'MAPK' -> 'mitogen-activated protein kinase' |
| Tissue | Serum |
| Organ | Endoderm |
| TextRef | info:pmid/12814546#body:217 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Curr Biol |
| MedLine Reference | 12814546:1216 |
| Sentence | Overexpression of Pyst1 Decreases Levels of Activated mitogen-activated protein kinase in Neural Plate . (A) EGFP-tagged Pyst1 dephosphorylates ERK in Cos1 cells. (B) Fibroblast growth factor4, but not (C) PBS beads (asterisks) locally increase levels of activated mitogen-activated protein kinase (detected with anti-dual-phosphorylated mitogen-activated protein kinase antibody, brown labeling) in the neural plate. (D and E) Levels of activated mitogen-activated protein kinase following electroporation. (D-D") Cells expressing Pyst1-EGFP (green) and activated mitogen-activated protein kinase (brown) were scored in Transverse section (red arrowheads, Pyst1-EGFP cells with low activated mitogen-activated protein kinase). |
| TextMods | 54: 'MAPK ' -> 'mitogen-activated protein kinase ' 167: 'FGF' -> 'Fibroblast growth factor' 265: 'MAPK ' -> 'mitogen-activated protein kinase ' 338: 'MAPK ' -> 'mitogen-activated protein kinase ' 448: 'MAPK ' -> 'mitogen-activated protein kinase ' 565:... |
| Organ | Neural Plate |