| URN | urn:agi-ProtModification:inout-urn:agi-llid:156:out-urn:agi-llid:154::unknown |
|---|---|
| References | 22 |
| Connectivity | 2 |
| Effect | unknown |
| TextRef | info:pmid/11087685#abs:10 |
|---|---|
| MedLine Reference | 11087685:9 |
| Sentence | GRK2 catalyzed modest phosphorylation of BAC1. |
| TextRef | info:pmid/1517224#abs:2 |
|---|---|
| MedLine Reference | 1517224:1 |
| Sentence | However, the capacity of beta ARK-phosphorylated beta 2AR to stimulate Gs in a reconstituted system is only minimally impaired. |
| TextRef | info:pmid/7673171#abs:3 |
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| MedLine Reference | 7673171:2 |
| Sentence | Using a mixed micelle assay, GRK2 (beta ARK1) was found to require phospholipid in order to phosphorylate the beta 2-adrenergic receptor. |
| TextRef | info:pmid/9010620#abs:1 |
|---|---|
| MedLine Reference | 9010620:0 |
| Sentence | Although its detailed substrate specificity is not precisely known, beta-adrenergic receptor kinase 1 phosphorylates beta 2-adrenergic receptors and other G protein-coupled receptors. |
| TextRef | info:pmid/8175732#abs:1 |
|---|---|
| MedLine Reference | 8175732:0 |
| Sentence | The beta-adrenergic receptor kinase (beta ARK) specifically phosphorylates the activated form of the beta 2-adrenergic receptor (beta 2AR) and related G protein-coupled receptors. |
| TextRef | info:pmid/16856836#abs:3 |
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| MedLine Reference | 16856836:2 |
| Sentence | Rolipram also facilitated GRK2 recruitment to the membrane and phosphorylation of the beta(2)Ar by GRK2 in response to isoprenaline challenge of cells. |
| Organ | kidney |
| Organism | Homo sapiens |
| TextRef | info:pmid/8393441#abs:1 |
|---|---|
| MedLine Reference | 8393441:0 |
| Sentence | The beta-adrenergic receptor kinase (beta-ARK) specifically phosphorylates the activated form of various G protein-coupled receptors such as the beta 2-adrenergic receptor (beta 2-AR). |
| TextRef | info:pmid/8170959#abs:8 |
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| CellLineName | Sf9 |
| MedLine Reference | 8170959:7 |
| Sentence | While phosphorylation of the beta 2-AR by GRK2, -3, and -5 is similar, the activity of GRK2 and -3 is enhanced by G beta gamma whereas that of GRK5 is not. |
| TextRef | info:pmid/1325672#abs:1 |
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| MedLine Reference | 1325672:0 |
| Sentence | The rate and extent of the agonist-dependent phosphorylation of beta 2-adrenergic receptors and rhodopsin by beta-adrenergic receptor kinase (beta ARK) are markedly enhanced on addition of G protein beta gamma subunits. |
| TextRef | info:pmid/9477943#abs:7 |
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| MedLine Reference | 9477943:6 |
| Sentence | The lack of a strong stimulatory effect of G beta gamma on GRK2-catalyzed phosphorylation of hSPR is surprising since G beta gamma potently stimulates GRK2-catalyzed phosphorylation of beta 2-adrenergic receptor and rhodopsin. |
| TextRef | info:pmid/1664548#abs:1 |
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| MedLine Reference | 1664548:0 |
| Sentence | Rhodopsin kinase and the beta-adrenergic receptor kinase (beta ARK) catalyse the phosphorylation of the activated forms of the G-protein-coupled receptors, rhodopsin and the beta 2-adrenergic receptor (beta 2AR), respectively. |
| TextRef | info:pmid/8381352#abs:2 |
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| MedLine Reference | 8381352:1 |
| Sentence | Agonist-promoted phosphorylation of the beta 2-adrenergic receptor (beta 2AR) by protein kinase A and the beta-adrenergic receptor kinase (beta ARK) is believed to promote a functional uncoupling of the receptor from the guanyl nucleotide regulatory protein Gs. |
| TextRef | info:pmid/8248128#abs:3 |
|---|---|
| CellLineName | Sf9 |
| MedLine Reference | 8248128:2 |
| Sentence | To investigate the specificity of this effect, we have purified various combinations of recombinant beta and gamma subunits expressed in Sf9 cells and measured their effects on beta ARK-catalyzed phosphorylation of beta 2-adrenergic receptors and of rhodopsin. |
| TextRef | info:pmid/16356165#abs:4 |
|---|---|
| MedLine Reference | 16356165:3 |
| Sentence | PDE4-selective inhibition by rolipram facilitates the isoprenaline-induced membrane translocation of GRK2, phosphorylation of the beta2AR by GRK2, membrane translocation of beta-arrestin and internalization of beta2ARs. |
| Organ | kidney |
| Organism | Homo sapiens |
| TextRef | info:pmid/8195124#abs:1 |
|---|---|
| MedLine Reference | 8195124:0 |
| Sentence | The beta-adrenergic receptor kinase (beta ARK) specifically phosphorylates the agonist-occupied forms of the beta 2-adrenergic receptor and related G protein-coupled receptors. beta ARK is one of the best characterized members of a growing family of G protein-coupled receptor kinases. |
| TextRef | info:pmid/18056263#abs:7 |
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| CellLineName | epi |
| MedLine Reference | 18056263:6 |
| Sentence | Subsequent studies showed that the Epi-activated beta(2)AR underwent a rapid phosphorylation by G protein-coupled receptor kinase 2 (GRK2) and subsequent dephosphorylation on serine residues 355 and 356, which was critical for sufficient receptor recycling and G(i) coupling. |
| CellType | cardiomyocyte |
| Organ | heart |
| TextRef | info:pmid/11146000#abs:1 |
|---|---|
| MedLine Reference | 11146000:0 |
| Sentence | Although palmitoylation of the beta(2)-adrenergic receptor (beta(2)AR), as well as its phosphorylation by the cyclic AMP-dependant protein kinase (PKA) and the beta-adrenergic receptor kinase (beta ARK), are known to play important roles in agonist-promoted desensitization, their relative contribution and mutual regulatory influences are still poorly understood. |
| TextRef | info:pmid/7556195#abs:7 |
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| MedLine Reference | 7556195:6 |
| Sentence | On the basis of these data, the binding of purified beta-arrestin to beta ARK-phosphorylated beta 2-adrenergic receptors was found to occur with a KD of 1.8 nM and with a maximum of 1 beta-arrestin/receptor. beta-arrestin also bound to receptors which had been completely dephosphorylated with acid phosphatase, but the affinity was approximately 30-fold lower. |
| TextRef | info:pmid/8096517#abs:1 |
|---|---|
| MedLine Reference | 8096517:0 |
| Sentence | The beta-adrenergic receptor kinase (beta ARK) specifically phosphorylates the activated form of multiple receptors such as the beta 2-adrenergic receptor (beta 2 AR) and rhodopsin. beta ARK also phosphorylates synthetic peptides, albeit with an approximately 10(4)-10(7)-fold lower Vmax/Km ratio as compared to receptors, with a clear preference for peptides containing acidic residues on the aminoterminal side of a serine or threonine. |
| TextRef | info:pmid/9151775#cont:9 |
|---|---|
| Journal | J Clin Invest |
| Journal Reference | v99 i9 p2060 |
| Journal Link | http://www.jci.org/cgi/content/full/99/9/2060 |
| MedLine Reference | 9151775:10008 |
| Sentence | In particular, phosphorylation of the ß 2 AR by ßARK has been shown to play a key role in the development of rapid agonistinduced desensitization (for review see references 2 and 3 ). |
| TextRef | info:pmid/9927627#cont:28 |
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| Journal | Mol. Pharm |
| Journal Reference | v55 i2 p339 |
| Journal Link | http://molpharm.aspetjournals.org/cgi/content/full/55/2/339 |
| MedLine Reference | 9927627:10027 |
| Sentence | This hypothesis is supported by previous findings that indicated that constitutively active beta -2 AR and alpha -2 AR carrying mutations in the distal portion of i3 loop can be phosphorylated by GRK2 in the absence of the agonist (Ren et al., 1993 ; Pei et al., 1994 ). |
| TextRef | info:pmid/12525498#cont:121 |
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| Journal | J. Biol. Chem |
| Journal Reference | v278 i13 p11623 |
| Journal Link | http://www.jbc.org/cgi/content/full/278/13/11623 |
| MedLine Reference | 12525498:10120 |
| Sentence | These functional characteristics of arrestin2(R169E) suggest that upon its overexpression in cells the phosphorylation of beta2AR by endogenous GRK2 will be attenuated and that unphosphorylated eta2AR will form complexes with the mutant arrestin2, which are likely to dissociate upon receptor deactivation due to agonist loss in endosomes faster than the complexes of WT arrestin2 with phosphorylated beta2AR. |
| Organ | brain |
| Organism | Homo sapiens |