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ARF与β-COP与高尔基体膜的结合:三聚体G蛋白的可能调控作用。

Binding of ARF and beta-COP to Golgi membranes: possible regulation by a trimeric G protein.

作者信息

Donaldson J G, Kahn R A, Lippincott-Schwartz J, Klausner R D

机构信息

Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.

出版信息

Science. 1991 Nov 22;254(5035):1197-9. doi: 10.1126/science.1957170.

Abstract

The binding of cytosolic coat proteins to organelles may regulate membrane structure and traffic. Evidence is presented that a small guanosine triphosphate (GTP)-binding protein, the adenosine diphosphate ribosylation factor (ARF), reversibly associates with the Golgi apparatus in an energy, GTP, and fungal metabolite brefeldin A (BFA)-sensitive manner similar to, but distinguishable from, the 110-kilodalton cytosolic coat protein beta-COP. Addition of beta gamma subunits of G proteins inhibited the association of both ARF and beta-COP with Golgi membranes that occurred upon incubation with guanosine 5'-O-(3-thiotriphosphate) (GTP-gamma-S). Thus, heterotrimeric G proteins may function to regulate the assembly of coat proteins onto the Golgi membrane.

摘要

胞质衣被蛋白与细胞器的结合可能会调节膜结构和运输。有证据表明,一种小的鸟苷三磷酸(GTP)结合蛋白,即二磷酸腺苷核糖基化因子(ARF),以一种对能量、GTP和真菌代谢产物布雷菲德菌素A(BFA)敏感的方式可逆地与高尔基体结合,这种方式与110千道尔顿的胞质衣被蛋白β-COP相似但又有区别。添加G蛋白的βγ亚基可抑制在与鸟苷5'-O-(3-硫代三磷酸)(GTP-γ-S)孵育时发生的ARF和β-COP与高尔基体膜的结合。因此,异源三聚体G蛋白可能起到调节衣被蛋白在高尔基体膜上组装的作用。

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