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Vol. 54, Issue 3, 527-559, September 2002
Department of Pharmacology, Emory University School of Medicine,
Atlanta, Georgia
I. Introduction
II. RGS Proteins Directly Regulate G Protein Activity
A. G Protein Activation and Deactivation and Early Evidence for RGS
Proteins
B. Discovery of RGS Proteins
C. RGS Proteins Are GTPase-Activating Proteins for G
D. Structure and Classification of RGS Proteins
E. Simple versus Complex RGS Proteins
III. RGS Proteins Modulate G Protein Signaling
A. RGS4 Modulation of Gq/11-Directed Ca2+
Signaling
1. Cellular Mechanisms That Influence RGS4 Membrane Recruitment and
Attachment.
2. Once Bound to Membranes, What Factors Influence RGS4 Specificity
for Target G in Cells?
3. Once RGS4 Is Bound to Membranes and Functionally Linked to
Receptor and G Protein, What Factors Regulate Its Effects on
Ca2+ Signaling?
4. What Factors Contribute to Turning Off This Signaling
Loop?
B. RGS4 As a Possible Scaffolding Protein That Links Receptors to
Related Signaling Proteins
C. RGS Modulation of the Kinetics of Fast-Acting Signaling
Responses
IV. RGS Proteins Integrate G Protein Signals
A. RGS Proteins Integrate Distinct G Protein Signaling Pathways
B. RGS Proteins Integrate G Protein and Non-G Protein-Linked
Signals
C. RGS Proteins Link G to Monomeric GTPases
D. RGS Proteins As Scaffolds to Assemble Related Signaling
Components
E. RGS Proteins Regulate Intracellular Trafficking
F. RGS Protein Interactions with Non-G Protein Binding Partners
V. Cellular Mechanisms Regulating RGS Protein Functions
A. Regulation of RGS Signaling Capacity by Feedback Phosphorylation
B. Membrane Targeting and Lipid Modification
C. Factors Regulating RGS Protein Half-Life
D. Targeted Subcellular Localization of RGS Proteins
E. Factors Regulating Cellular Expression of RGS Proteins
F. Expression of Alternatively Spliced Gene Products
VI. RGS Proteins As Therapeutic Targets
A. Roles for RGS Proteins in Cell Migration and Development
B. Roles of RGS Proteins in Organ Physiology
C. RGS Proteins in Neuronal Function and Behavior
D. RGS Proteins in Disease States
E. Molecular Targets for Drug Development
1. Direct Modulation of RGS/G Binding.
2. Allosteric Modulation of RGS/G Binding.
3. Selectivity of RGS-G Interactions.
4. Modulation of RGS Membrane Localization.
5. Modulation of RGS Binding to GPCR, Effector and/or Regulatory
Proteins.
VII. Conclusion and Future Directions
Acknowledgments
References
Regulators of G protein signaling (RGS) and RGS-like proteins are a
family (>30 members) of highly diverse, multifunctional signaling
proteins that bind directly to activated G subunits. Family members
are defined by a shared RGS domain, which is responsible for G
binding and markedly stimulates the GTPase activity of G subunits
leading to their deactivation and termination of downstream signals.
Although much has been learned in recent years about the biochemistry
of RGS/G interactions, considerably less is known about the broader
cellular roles and regulation of RGS proteins. Recent findings indicate
that cellular mechanisms such as covalent modification, alternative
gene splicing, and protein processing can dictate the activity and
subcellular localization of RGS proteins. Many family members also
directly link G proteins to a growing list of signaling proteins with
diverse cellular roles. New findings indicate that RGS proteins act not
as dedicated inhibitors but, rather, as tightly regulated modulators
and integrators of G protein signaling. In some cases, RGS proteins
modulate the lifetime and kinetics of both slow-acting (e.g.,
Ca2+ oscillations) and fast-acting (e.g., ion conductances,
phototransduction) signaling responses. In other cases, RGS proteins
integrate G proteins with signaling pathways linked to such diverse
cellular responses as cell growth and differentiation, cell motility,
and intracellular trafficking. These and other recent studies with animal model systems indicate that RGS proteins play important roles in
both physiology and disease. Recognition of the central functions these
proteins play in vital cellular processes has focused our attention on
RGS proteins as exciting new candidates for therapeutic intervention
and drug development.
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