期刊
MOLECULAR PHARMACOLOGY
卷 78, 期 4, 页码 550-557出版社
AMER SOC PHARMACOLOGY EXPERIMENTAL THERAPEUTICS
DOI: 10.1124/mol.110.065219
关键词
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资金
- National Institutes of Health National Institute of General Medical Sciences [R01-GM39561]
- Swedish Research council [VR-524-2008-6963]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM039561] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE ON DRUG ABUSE [R01DA023252] Funding Source: NIH RePORTER
Regulators of G protein signaling (RGS) proteins are emerging as potentially important drug targets. The mammalian RGS protein family has more than 20 members and they share a common similar to 120-residue RGS homology domain or RGS box. RGS proteins regulate signaling via G protein-coupled receptors by accelerating GTPase activity at active alpha subunits of G proteins of the G(q) and G(i/o) families. Most studies searching for modulators of RGS protein function have been focused on inhibiting the GTPase accelerating protein activity. However, many RGS proteins contain additional domains that serve other functions, such as interactions with proteins or subcellular targeting. Here, we discuss a rationale for therapeutic targeting of RGS proteins by regulation of expression or allosteric modulation to permit either increases or decreases in RGS function. Several RGS proteins have reduced expression or function in pathophysiological states, so strategies to increase RGS function would be useful. Because several RGS proteins are rapidly degraded by the N-end rule pathway, finding ways to stabilize them may prove to be an effective way to enhance RGS protein function.
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