Specificity of G protein-RGS protein recognition is regulated by affinity adapters
Specificity of G protein-RGS protein recognition is regulated by affinity adapters
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DOI：
10.1016/s0896-6273(03)00320-9
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发表时间：
2003-06-19
期刊：
影响因子：
16.2
通讯作者：
Arshavsky, VY
中科院分区：
文献类型：
--
作者：
Martemyanov, KA;Hopp, JA;Arshavsky, VY
RGS proteins regulate the duration of cell signaling by modulating the lifetime of activated G proteins. The specificity of RGS-G protein mutual recognition is critical for meeting unique timing requirements of numerous G protein-mediated pathways. Our study of two splice isoforms of RGS9 expressed in different types of neurons revealed a novel mechanism whereby this specificity is determined by specialized protein domains or subunits acting as affinity adapters. The long RGS9 isoform contains a C-terminal domain that provides high-affinity interaction with its target G protein. The lack of this domain in the short RGS9 isoform is compensated by the action of a G protein effector subunit that is structurally similar to this C-terminal domain. This allows the short isoform to specifically target the complex between the G protein and its effector. Thus, the specific timing needs of different signaling pathways can be accommodated by affinity adapters positioned at various pathway components.
