PMID- 10339615
OWN - NLM
STAT- MEDLINE
DCOM- 19990624
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 11
DP  - 1999 May 25
TI  - Fidelity of G protein beta-subunit association by the G protein
      gamma-subunit-like domains of RGS6, RGS7, and RGS11.
PG  - 6489-94
AB  - Several regulators of G protein signaling (RGS) proteins contain a G protein
      gamma-subunit-like (GGL) domain, which, as we have shown, binds to Gbeta5
      subunits. Here, we extend our original findings by describing another
      GGL-domain-containing RGS, human RGS6. When RGS6 is coexpressed with different
      Gbeta subunits, only RGS6 and Gbeta5 interact. The expression of mRNA for RGS6
      and Gbeta5 in human tissues overlaps. Predictions of alpha-helical and
      coiled-coil character within GGL domains, coupled with measurements of Gbeta
      binding by GGL domain mutants, support the contention that Ggamma-like regions
      within RGS proteins interact with Gbeta5 subunits in a fashion comparable to
      conventional Gbeta/Ggamma pairings. Mutation of the highly conserved Phe-61
      residue of Ggamma2 to tryptophan, the residue present in all GGL domains,
      increases the stability of the Gbeta5/Ggamma2 heterodimer, highlighting the
      importance of this residue to GGL/Gbeta5 association.
FAU - Snow, B E
AU  - Snow BE
AD  - Amgen Institute, Toronto, ON, Canada M5G2C1.
FAU - Betts, L
AU  - Betts L
FAU - Mangion, J
AU  - Mangion J
FAU - Sondek, J
AU  - Sondek J
FAU - Siderovski, D P
AU  - Siderovski DP
LA  - eng
SI  - GENBANK/AF107619
SI  - GENBANK/AF107620
PT  - Journal Article
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 (DNA, Complementary)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Proteins)
RN  - 0 (RGS Proteins)
RN  - 0 (RGS7 protein, human)
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Proteins)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - COS Cells
MH  - DNA, Complementary
MH  - GTP-Binding Proteins/chemistry/genetics/*metabolism
MH  - Humans
MH  - Macromolecular Substances
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Biosynthesis
MH  - Protein Conformation
MH  - Proteins/chemistry/genetics/*metabolism
MH  - *RGS Proteins
MH  - RNA, Messenger/genetics
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Transcription, Genetic
MH  - Transfection
PMC - PMC26909
EDAT- 1999/05/26 00:00
MHDA- 1999/05/26 00:01
CRDT- 1999/05/26 00:00
PHST- 1999/05/26 00:00 [pubmed]
PHST- 1999/05/26 00:01 [medline]
PHST- 1999/05/26 00:00 [entrez]
AID - 10.1073/pnas.96.11.6489 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 May 25;96(11):6489-94. doi:
      10.1073/pnas.96.11.6489.