G Protein β Subunit Types Differentially Interact with a Muscarinic Receptor but Not Adenylyl Cyclase Type II or Phospholipase C-β2/3
In comparison with the α subunit of G proteins, the role of the β subunit in signaling is less well understood. During the regulation of effectors by the βγ complex, it is known that the β subunit contacts effectors directly, whereas the role of the β subunit is undefined in receptor-G protein inter...
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Veröffentlicht in: | The Journal of biological chemistry 2001-01, Vol.276 (23), p.19982-19988 |
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container_title | The Journal of biological chemistry |
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creator | Hou, Yongmin Chang, Vanessa Capper, Austin B. Taussig, Ronald Gautam, N. |
description | In comparison with the α subunit of G proteins, the role of the β subunit in signaling is less well understood. During the regulation of effectors by the βγ complex, it is known that the β subunit contacts effectors directly, whereas the role of the β subunit is undefined in receptor-G protein interaction. Among the five G protein β subunits known, the β4subunit type is the least studied. We compared the ability of βγ complexes containing β4 and the well characterized β1 to stimulate three different effectors: phospholipase C-β2, phospholipase C-β3, and adenylyl cyclase type II. β4γ2 and β1γ2 activated all three of these effectors with equal efficacy. However, nucleotide exchange in a G protein constituting αoβ4γ2 was stimulated significantly more by the M2 muscarinic receptor compared with αoβ1γ2. Because αo forms heterotrimers with β4γ2 and β1γ2equally well, these results show that the β subunit type plays a direct role in the receptor activation of a G protein. |
doi_str_mv | 10.1074/jbc.M010424200 |
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title | G Protein β Subunit Types Differentially Interact with a Muscarinic Receptor but Not Adenylyl Cyclase Type II or Phospholipase C-β2/3 |
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