Kuner R, Köhr G, Grünewald S, Eisenhardt G, Bach A, Kornau H C
BASF-LYNX Bioscience AG, Department of Neuroscience, Im Neuenheimer Feld 515, D-69120 Heidelberg, Germany.
Science. 1999 Jan 1;283(5398):74-7. doi: 10.1126/science.283.5398.74.
Recently, GBR1, a seven-transmembrane domain protein with high affinity for gamma-aminobutyric acid (GABA)B receptor antagonists, was identified. Here, a GBR1-related protein, GBR2, was shown to be coexpressed with GBR1 in many brain regions and to interact with it through a short domain in the carboxyl-terminal cytoplasmic tail. Heterologously expressed GBR2 mediated inhibition of adenylyl cyclase; however, inwardly rectifying potassium channels were activated by GABAB receptor agonists only upon coexpression with GBR1 and GBR2. Thus, the interaction of these receptors appears to be crucial for important physiological effects of GABA and provides a mechanism in receptor signaling pathways that involve a heterotrimeric GTP-binding protein.
最近，人们鉴定出了GBR1，一种对γ-氨基丁酸（GABA）B受体拮抗剂具有高亲和力的七跨膜结构域蛋白。在此，一种与GBR1相关的蛋白GBR2被证明在许多脑区与GBR1共表达，并通过羧基末端胞质尾中的一个短结构域与之相互作用。异源表达的GBR2介导了对腺苷酸环化酶的抑制作用；然而，内向整流钾通道仅在与GBR1和GBR2共表达时才被GABAB受体激动剂激活。因此，这些受体之间的相互作用似乎对GABA的重要生理效应至关重要，并在涉及异源三聚体GTP结合蛋白的受体信号通路中提供了一种机制。
