PMID- 9278091
OWN - NLM
STAT- MEDLINE
DCOM- 19970910
LR  - 20190623
IS  - 0006-2952 (Print)
IS  - 0006-2952 (Linking)
VI  - 54
IP  - 3
DP  - 1997 Aug 1
TI  - Role of subunit diversity in signaling by heterotrimeric G proteins.
PG  - 325-39
AB  - The heterotrimeric G proteins are extensively involved in the regulation of cells 
      by extracellular signals. The receptors that control them are often the targets 
      of drugs. There are many isoforms of each of the three subunits that make up 
      these proteins. Thus far, genes for at least sixteen alpha subunits, five beta 
      subunits, and eleven gamma subunits have been identified. In addition, some of 
      these proteins have splice variants or are differentially modified. Based upon 
      what is already known, there are well over a thousand possible G protein 
      heterotrimer combinations. The role of subunit diversity in heterotrimer 
      formation and its effect on signaling by G proteins are still not well 
      understood. However, many current lines of research are leading toward an 
      understanding of these roles. The functional significance of subunit 
      heterogeneity is related to the mechanisms used by G proteins to transmit and 
      integrate the many signals coming into cells through this system. Described here 
      are the basic mechanisms by which G proteins integrate cellular responses, the 
      possible role of subunit heterogeneity in these mechanisms, and the evidence for 
      and against their physiological significance. Recent studies suggest the likely 
      possibility that subunit heterogeneity plays an important role in signaling by G 
      proteins. This role has the potential to extend substantially the flexibility of 
      G proteins in mediating cellular responses to extracellular signals. However, the 
      details of this are yet to be worked out, and they are the subject of many 
      different avenues of research.
FAU - Hildebrandt, J D
AU  - Hildebrandt JD
AD  - Department of Cell and Molecular Pharmacology, Medical University of South 
      Carolina, Charleston 29425-2251, U.S.A. hildebjd@musc.edu
LA  - eng
SI  - GENBANK/L34290
SI  - GENBANK/P02698
SI  - GENBANK/P04895
SI  - GENBANK/P04899
SI  - GENBANK/P04901
SI  - GENBANK/P08754
SI  - GENBANK/P09471
SI  - GENBANK/P10824
SI  - GENBANK/P11016
SI  - GENBANK/P11488
SI  - GENBANK/P16520
SI  - GENBANK/P19085
SI  - GENBANK/P19086
SI  - GENBANK/P21278
SI  - GENBANK/P21279
SI  - GENBANK/P27600
SI  - GENBANK/P27601
SI  - GENBANK/P29348
SI  - GENBANK/P29387
SI  - GENBANK/P29777
SI  - GENBANK/P30670
SI  - GENBANK/P30671
SI  - GENBANK/P30677
SI  - GENBANK/P30678
SI  - GENBANK/P30679
SI  - GENBANK/P38405
SI  - GENBANK/U20085
SI  - GENBANK/U31383
SI  - GENBANK/U31384
SI  - GENBANK/U37561
GR  - DK32719/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - England
TA  - Biochem Pharmacol
JT  - Biochemical pharmacology
JID - 0101032
RN  - 0 (Receptors, Cell Surface)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - Cell Line
MH  - GTP-Binding Proteins/chemistry/genetics/*metabolism
MH  - Humans
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Receptors, Cell Surface/metabolism
MH  - *Signal Transduction
RF  - 229
EDAT- 1997/08/01 00:00
MHDA- 1997/08/01 00:01
CRDT- 1997/08/01 00:00
PHST- 1997/08/01 00:00 [pubmed]
PHST- 1997/08/01 00:01 [medline]
PHST- 1997/08/01 00:00 [entrez]
AID - S0006-2952(97)00269-4 [pii]
AID - 10.1016/s0006-2952(97)00269-4 [doi]
PST - ppublish
SO  - Biochem Pharmacol. 1997 Aug 1;54(3):325-39. doi: 10.1016/s0006-2952(97)00269-4.