Specificity of G protein-RGS protein recognition is regulated by affinity adapters |
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Authors: | Martemyanov Kirill A Hopp Johnathan A Arshavsky Vadim Y |
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Institution: | Howe Laboratory of Ophthalmology, Harvard Medical School, The Massachusetts Eye and Ear Infirmary, Boston, MA 02114, USA. |
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Abstract: | 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. |
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