PMID- 1325672
OWN - NLM
STAT- MEDLINE
DCOM- 19921006
LR  - 20240109
IS  - 0036-8075 (Print)
IS  - 0036-8075 (Linking)
VI  - 257
IP  - 5074
DP  - 1992 Aug 28
TI  - Role of beta gamma subunits of G proteins in targeting the beta-adrenergic 
      receptor kinase to membrane-bound receptors.
PG  - 1264-7
AB  - 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. With a model 
      peptide substrate it was demonstrated that direct activation of the kinase could 
      not account for this effect. G protein beta gamma subunits were shown to interact 
      directly with the COOH-terminal region of beta ARK, and formation of this beta 
      ARK-beta gamma complex resulted in receptor-facilitated membrane localization of 
      the enzyme. The beta gamma subunits of transducin were less effective at both 
      enhancing the rate of receptor phosphorylation and binding to the COOH-terminus 
      of beta ARK, suggesting that the enzyme preferentially binds specific beta gamma 
      complexes. The beta gamma-mediated membrane localization of beta ARK serves to 
      intimately link receptor activation to beta ARK-mediated desensitization.
FAU - Pitcher, J A
AU  - Pitcher JA
AD  - Howard Hughes Medical Research Institute, Department of Medicine, Duke University 
      Medical Center, Durham, NC 27710.
FAU - Inglese, J
AU  - Inglese J
FAU - Higgins, J B
AU  - Higgins JB
FAU - Arriza, J L
AU  - Arriza JL
FAU - Casey, P J
AU  - Casey PJ
FAU - Kim, C
AU  - Kim C
FAU - Benovic, J L
AU  - Benovic JL
FAU - Kwatra, M M
AU  - Kwatra MM
FAU - Caron, M G
AU  - Caron MG
FAU - Lefkowitz, R J
AU  - Lefkowitz RJ
LA  - eng
GR  - 4R37-HL16039/HL/NHLBI NIH HHS/United States
GR  - GM 44944/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Science
JT  - Science (New York, N.Y.)
JID - 0404511
RN  - 0 (Receptors, Adrenergic, beta)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Virulence Factors, Bordetella)
RN  - 9009-81-8 (Rhodopsin)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
RN  - EC 2.7.11.15 (beta-Adrenergic Receptor Kinases)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cattle
MH  - *Cyclic AMP-Dependent Protein Kinases
MH  - Dose-Response Relationship, Drug
MH  - Escherichia coli
MH  - GTP-Binding Proteins/*physiology
MH  - Gene Expression Regulation/drug effects
MH  - In Vitro Techniques
MH  - Molecular Sequence Data
MH  - Phosphorylation
MH  - Protein Kinases/*pharmacology
MH  - Protein Processing, Post-Translational
MH  - Receptors, Adrenergic, beta/*drug effects/*metabolism
MH  - Recombinant Fusion Proteins
MH  - Rhodopsin/metabolism
MH  - Time Factors
MH  - Virulence Factors, Bordetella/pharmacology
MH  - beta-Adrenergic Receptor Kinases
EDAT- 1992/08/28 00:00
MHDA- 1992/08/28 00:01
CRDT- 1992/08/28 00:00
PHST- 1992/08/28 00:00 [pubmed]
PHST- 1992/08/28 00:01 [medline]
PHST- 1992/08/28 00:00 [entrez]
AID - 10.1126/science.1325672 [doi]
PST - ppublish
SO  - Science. 1992 Aug 28;257(5074):1264-7. doi: 10.1126/science.1325672.