| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| Surprisingly , expression of beta arrestin 1 ( V53D ) does not block activation of the MAPK ( ERK ) pathway . ^^^ |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| Src recruitment was mediated by beta arrestin , which functions as an adapter protein , binding both c Src and the agonist occupied receptor . beta Arrestin 1 mutants , impaired either in c Src binding or in the ability to target receptors to clathrin coated pits , acted as dominant negative inhibitors of beta 2 adrenergic receptor mediated activation of the MAP kinases Erk 1 and Erk 2 . ^^^ |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| The functions of beta arrestin 1 to facilitate clathrin mediated endocytosis of the beta 2 adrenergic receptor and to promote agonist induced activation of extracellular signal regulated kinases ( ERK ) are regulated by its phosphorylation / dephosphorylation at Ser 412 . ^^^ Here we demonstrate that beta arrestin 1 phosphorylation and function are modulated by an ERK dependent negative feedback mechanism . ^^^ ERK 1 and ERK 2 phosphorylate beta arrestin 1 at Ser 412 in vitro . ^^^ Inhibition of ERK activity by a dominant negative MEK 1 mutant significantly attenuates beta arrestin 1 phosphorylation , thereby increasing the concentration of dephosphorylated beta arrestin 1 . ^^^ Our results suggest that dephosphorylated beta arrestin 1 mediates endocytosis dependent ERK activation . ^^^ |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| Surprisingly , we found that in COS 7 cells , ERK activation by the alpha ( 2A ) AR , like that mediated by both the beta ( 2 ) AR and the epidermal growth factor receptor ( EGFR ) , is sensitive to mechanistically distinct inhibitors of clathrin mediated endocytosis , including monodansylcadaverine , a mutant dynamin 1 , and a mutant beta arrestin 1 . ^^^ |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| We previously showed that c Src is required for ERK activation by beta ( 2 ) AR and that it is recruited to activated beta ( 2 ) AR through binding of the Src homology 3 ( SH 3 ) domain to proline rich regions of the adapter protein beta arrestin 1 . ^^^ |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| In contrast to beta arrestin 1 , which is phosphorylated by ERK 1 and ERK 2 , phosphorylation of beta arrestin 2 at Thr 383 is shown to be mediated by casein kinase 2 . ^^^ |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| These results are the first to demonstrate reciprocal activity of beta arrestin isoforms on a signaling pathway and suggest that physiological levels of beta arrestin 1 may act as `` dominant negative ' ' inhibitors of beta arrestin 2 mediated ERK activation . . ^^^ |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| Insulin induced beta arrestin 1 Ser 412 phosphorylation is a mechanism for desensitization of ERK activation by Galphai coupled receptors . ^^^ Phosphorylation of beta arrestin 1 at position Ser 412 is a regulator of beta arrestin 1 function , and in the present study , we showed that insulin led to a time and dose dependent increase in beta arrestin 1 Ser 412 phosphorylation , which blocked isoproterenol and lysophosphatidic acid induced Ser 412 dephosphorylation and impaired ERK signaling by these G protein coupled receptor ligands . ^^^ |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| Paired activation of two components within muscarinic M 3 receptor dimers is required for recruitment of beta arrestin 1 to the plasma membrane . beta Arrestins regulate the functioning of G protein coupled receptors in a variety of cellular processes including receptor mediated endocytosis and activation of signaling molecules such as ERK . ^^^ |
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| Interacting proteins: P49407 and P28482 |
Pubmed |
SVM Score :0.0 |
| Likewise , overexpression of wild type beta arrestin 1 or 2 significantly increased the FSH R internalization level in response to FSH , without altering FSH induced ERK phosphorylation . ^^^ |
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