Gsalpha contains an unidentified covalent modification that increases its affinity for adenylyl cyclase.
Gsalpha contains an unidentified covalent modification that increases its affinity for adenylyl cyclase.
复制标题
Gsalpha 含有一种未鉴定的共价修饰，可增加其对腺苷酸环化酶的亲和力。
DOI：
10.1073/pnas.94.12.6116
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发表时间：
1997
影响因子：
11.1
通讯作者：
Gilman,AG
中科院分区：
文献类型：
--
作者：
Kleuss,C;Gilman,AG
许多G蛋白α亚基被肉豆蔻酸酯和棕榈酸酯双重酰化，或者在N末端附近的一个以上半胱氨酸残基上被棕榈酰化。激活腺苷酸环化酶αs的Gα蛋白不是肉豆蔻酰化的，但可以可逆地棕榈酰化。似乎α s含有另一种尚未鉴定的共价修饰，其将腺苷酸环化酶的表观解离常数从50 nM降低至<0.5 nM。这种修饰位于或靠近蛋白质的N末端，并且是疏水性的。天然α s的棕榈酰化不能解释其对腺苷酸环化酶的高亲和力。
Many G protein α subunits are dually acylated with myristate and palmitate or are palmitoylated on more than one cysteine residue near their N termini. The Gαprotein that activates adenylyl cyclase, αs, is not myristoylated but can be reversibly palmitoylated. It appears that αscontains another, as-yet-unidentified covalent modification that decreases its apparent dissociation constant for adenylyl cyclase from 50 nM to <0.5 nM. This modification is at or near the N terminus of the protein and is hydrophobic. Palmitoylation of native αsdoes not account for its high affinity for adenylyl cyclase.