Benovic Jeffrey L
Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA 19107, USA.
J Allergy Clin Immunol. 2002 Dec;110(6 Suppl):S229-35. doi: 10.1067/mai.2002.129370.
The beta(2)-adrenergic receptor (beta(2)AR) is perhaps the most thoroughly investigated of all G-protein-coupled receptors. Although the classical pathway of beta(2)AR signaling involves agonist-promoted binding of the receptor to the heterotrimeric guanosine triphosphate-binding protein G(s), activation of adenylyl cyclase, and production of cyclic adenosine monophosphate (cAMP), current evidence suggests that beta(2)AR signaling is regulated by interaction with multiple proteins. These interactions fall into 3 major groups: guanosine triphosphate-binding proteins such as G(s) and G(i); protein kinases such as the cAMP-dependent protein kinase, protein kinase C, G-protein-coupled receptor kinases, and tyrosine kinases; and adaptor proteins such as arrestins, A-kinase anchoring proteins, and the Na(+)/H(+)-exchanger regulatory factor. This review discusses these various interactions with particular emphasis on their role in regulating beta(2)AR signaling and trafficking.
β₂肾上腺素能受体（β₂AR）可能是所有G蛋白偶联受体中研究最为深入的。虽然β₂AR信号传导的经典途径涉及激动剂促进受体与异三聚体鸟苷三磷酸结合蛋白Gₛ结合、腺苷酸环化酶激活以及环磷酸腺苷（cAMP）生成，但目前的证据表明β₂AR信号传导受与多种蛋白质相互作用的调节。这些相互作用分为三大类：鸟苷三磷酸结合蛋白，如Gₛ和Gᵢ；蛋白激酶，如cAMP依赖性蛋白激酶、蛋白激酶C、G蛋白偶联受体激酶和酪氨酸激酶；以及衔接蛋白，如抑制蛋白、A激酶锚定蛋白和钠/氢交换调节因子。本综述讨论了这些不同的相互作用，特别强调它们在调节β₂AR信号传导和转运中的作用。
