PMID- 10051672
OWN - NLM
STAT- MEDLINE
DCOM- 19990415
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 5
DP  - 1999 Mar 2
TI  - Gbeta5 prevents the RGS7-Galphao interaction through binding to a distinct
      Ggamma-like domain found in RGS7 and other RGS proteins.
PG  - 2503-7
AB  - The G protein beta subunit Gbeta5 deviates significantly from the other four
      members of Gbeta-subunit family in amino acid sequence and subcellular
      localization. To detect the protein targets of Gbeta5 in vivo, we have isolated a
      native Gbeta5 protein complex from the retinal cytosolic fraction and identified 
      the protein tightly associated with Gbeta5 as the regulator of G protein
      signaling (RGS) protein, RGS7. Here we show that complexes of Gbeta5 with RGS
      proteins can be formed in vitro from the recombinant proteins. The reconstituted 
      Gbeta5-RGS dimers are similar to the native retinal complex in their behavior on 
      gel-filtration and cation-exchange chromatographies and can be immunoprecipitated
      with either anti-Gbeta5 or anti-RGS7 antibodies. The specific Gbeta5-RGS7
      interaction is determined by a distinct domain in RGS that has a striking
      homology to Ggamma subunits. Deletion of this domain prevents the RGS7-Gbeta5
      binding, although the interaction with Galpha is retained. Substitution of the
      Ggamma-like domain of RGS7 with a portion of Ggamma1 changes its binding
      specificity from Gbeta5 to Gbeta1. The interaction of Gbeta5 with RGS7 blocked
      the binding of RGS7 to the Galpha subunit Galphao, indicating that Gbeta5 is a
      specific RGS inhibitor.
FAU - Levay, K
AU  - Levay K
AD  - Department of Molecular and Cellular Pharmacology and Neuroscience Program,
      University of Miami School of Medicine, Miami, FL 33136, USA.
FAU - Cabrera, J L
AU  - Cabrera JL
FAU - Satpaev, D K
AU  - Satpaev DK
FAU - Slepak, V Z
AU  - Slepak VZ
LA  - eng
SI  - GENBANK/AF073920
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Macromolecular Substances)
RN  - 0 (Proteins)
RN  - 0 (RGS Proteins)
RN  - 0 (Recombinant Proteins)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Chromatography, Gel
MH  - Chromatography, Ion Exchange
MH  - Cloning, Molecular
MH  - Cytosol/metabolism
MH  - Escherichia coli
MH  - GTP-Binding Proteins/chemistry/isolation & purification/*metabolism
MH  - Macromolecular Substances
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Proteins/chemistry/isolation & purification/*metabolism
MH  - *RGS Proteins
MH  - Rabbits
MH  - Recombinant Proteins/chemistry/isolation & purification/metabolism
MH  - Reticulocytes/metabolism
MH  - Retina/*metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
PMC - PMC26814
EDAT- 1999/03/03 00:00
MHDA- 1999/03/03 00:01
CRDT- 1999/03/03 00:00
PHST- 1999/03/03 00:00 [pubmed]
PHST- 1999/03/03 00:01 [medline]
PHST- 1999/03/03 00:00 [entrez]
AID - 10.1073/pnas.96.5.2503 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2503-7. doi: 10.1073/pnas.96.5.2503.