PMID- 10203790
OWN - NLM
STAT- MEDLINE
DCOM- 19990706
LR  - 20191024
IS  - 0962-8924 (Print)
IS  - 0962-8924 (Linking)
VI  - 9
IP  - 4
DP  - 1999 Apr
TI  - RGS proteins: more than just GAPs for heterotrimeric G proteins.
PG  - 138-44
AB  - Members of the newly described RGS family of proteins have a common RGS domain
      that contains GTPase-activating activity for many Galpha subunits of
      heterotrimeric G proteins. Their ability to dampen signalling via Galphai-,
      Galphaq- and Galpha12/13-coupled pathways makes them crucial players in mediating
      the multitude of cellular processes controlled by heterotrimeric G proteins. Some
      RGS proteins also contain additional motifs that link them to other signalling
      networks, where they constitute effector-type molecules. This review summarizes
      recent findings on RGS proteins, especially those that implicate RGS proteins in 
      more than just enhancing the GTPase activity of their Galpha subunit targets.
FAU - De Vries, L
AU  - De Vries L
AD  - Division of Cellular and Molecular Medicine, University of California, San Diego,
      La Jolla, CA 92093, USA. ldevries@ucsd.edu
FAU - Gist Farquhar, M
AU  - Gist Farquhar M
LA  - eng
GR  - CA58689/CA/NCI NIH HHS/United States
GR  - DK17780/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - England
TA  - Trends Cell Biol
JT  - Trends in cell biology
JID - 9200566
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Dishevelled Proteins)
RN  - 0 (GTPase-Activating Proteins)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Membrane Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (Proteins)
RN  - EC 3.6.1.- (GTP Phosphohydrolases)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
SB  - IM
MH  - Adaptor Proteins, Signal Transducing
MH  - Animals
MH  - Chemical Phenomena
MH  - Chemistry, Physical
MH  - Dishevelled Proteins
MH  - Drosophila melanogaster/metabolism
MH  - GTP Phosphohydrolases/*metabolism
MH  - GTP-Binding Proteins/*physiology
MH  - GTPase-Activating Proteins
MH  - Macromolecular Substances
MH  - Mammals/metabolism
MH  - Membrane Proteins/metabolism
MH  - Models, Biological
MH  - Multigene Family
MH  - Organ Specificity
MH  - Phosphoproteins/physiology
MH  - Protein Conformation
MH  - Proteins/classification/*physiology
MH  - Rats
MH  - Signal Transduction/*physiology
MH  - Structure-Activity Relationship
MH  - Subcellular Fractions/metabolism
MH  - Transcription, Genetic
RF  - 67
EDAT- 1999/05/04 00:00
MHDA- 1999/05/04 00:01
CRDT- 1999/05/04 00:00
PHST- 1999/05/04 00:00 [pubmed]
PHST- 1999/05/04 00:01 [medline]
PHST- 1999/05/04 00:00 [entrez]
AID - S0962-8924(99)01515-9 [pii]
AID - 10.1016/s0962-8924(99)01515-9 [doi]
PST - ppublish
SO  - Trends Cell Biol. 1999 Apr;9(4):138-44. doi: 10.1016/s0962-8924(99)01515-9.