The relationship of G(o)alpha subunit deamidation to the tissue distribution, nucleotide binding properties, and betagamma dimer interactions of G(o)alpha subunit isoforms.
The relationship of G(o)alpha subunit deamidation to the tissue distribution, nucleotide binding properties, and betagamma dimer interactions of G(o)alpha subunit isoforms.
复制标题
G(o)alpha 亚基脱酰胺与 G(o)alpha 亚基异构体的组织分布、核苷酸结合特性和 betaamma 二聚体相互作用的关系。
DOI：
10.1046/j.1471-4159.1999.0730633.x
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发表时间：
1999
影响因子：
4.7
通讯作者：
Hildebrandt,JD
中科院分区：
文献类型：
--
作者：
McIntire,WE;Dingus,J;Wilcox,MD;Hildebrandt,JD
Abstract: The distribution and properties in brain of the α subunits of the major bovine brain Goisoforms, GoA, GoBand GoC, were characterized. The αoAand αoBisoforms arise from alternative splicing of RNAs from a single αogene, whereas αoCis a deamidated form of αoA. All three Goisoforms purify from brain with different populations of βγ dimers. This variable subunit composition of Goheterotrimers is likely a consequence of their functional differences. This study examined the biochemical properties of the αoisoforms to see if these properties explain the variable βγ composition of their heterotrimers. The brain distribution of αoBdiffered substantially from that of αoAand αoC, as did its guanine nucleotide binding properties. The unique subunit composition of GoBcan be explained by its expression in different brain regions. The αoAand αoCshowed slight differences in guanine nucleotide binding properties but no preference for particular βγ dimers when reassociated with a heterogeneous βγ pool. The αoCprotein occurred in a constant ratio to αoAthroughtout the brain, but was a much larger percent of total brain αothan previously thought, ~35%. These results suggest that αoAis a precursor of αoCand that the association of Goα subunits with different βγ dimers reflects the function of an adaptive, G‐protein signaling mechanism in brain.
