Abramow-Newerly Maria, Roy Anju A, Nunn Caroline, Chidiac Peter
Department of Physiology and Pharmacology, University of Western Ontario, London, Ontario, Canada N6A 5C1.
Cell Signal. 2006 May;18(5):579-91. doi: 10.1016/j.cellsig.2005.08.010. Epub 2005 Oct 13.
The intracellular regulator of G protein signalling (RGS) proteins were first identified as GTPase activating proteins (GAPs) for heterotrimeric G proteins, however, it was later found that they can also regulate G protein-effector interactions in other ways that are still not well understood. There is increasing evidence that some of the effects of RGS proteins occur due to their ability to interact with multiprotein signalling complexes. In this review, we will discuss recent evidence that supports the idea that RGS proteins can bind to proteins other than Galpha, such as G protein coupled receptors (GPCRs, e.g. muscarinic, dopaminergic, adrenergic, angiotensin, interleukin and opioid receptors) and effectors (e.g. adenylyl cyclase, GIRK channels, PDEgamma, PLC-beta and Ca(2+) channels). Furthermore, we will investigate novel RGS binding partners (e.g. GIPC, spinophilin, 14-3-3) that underlie the formation of signalling scaffolds or govern RGS protein availability and/or activity.
G蛋白信号转导调节蛋白（RGS）最初被鉴定为异源三聚体G蛋白的GTP酶激活蛋白（GAP），然而，后来发现它们也能以其他尚不清楚的方式调节G蛋白与效应器的相互作用。越来越多的证据表明，RGS蛋白的某些作用是由于它们与多蛋白信号复合物相互作用的能力。在这篇综述中，我们将讨论最近的证据，这些证据支持RGS蛋白可以与Gα以外的蛋白质结合的观点，如G蛋白偶联受体（GPCR，如毒蕈碱、多巴胺能、肾上腺素能、血管紧张素、白细胞介素和阿片受体）和效应器（如腺苷酸环化酶、GIRK通道、PDEγ、PLC-β和Ca(2+)通道）。此外，我们将研究新型RGS结合伴侣（如GIPC、亲嗜素、14-3-3），它们是信号支架形成的基础，或控制RGS蛋白的可用性和/或活性。
