Stevens T H, Forgac M
Institute of Molecular Biology, University of Oregon, Eugene 97403-1229, USA.
Annu Rev Cell Dev Biol. 1997;13:779-808. doi: 10.1146/annurev.cellbio.13.1.779.
The vacuolar (H+)-ATPases (or V-ATPases) function in the acidification of intracellular compartments in eukaryotic cells. The V-ATPases are multisubunit complexes composed of two functional domains. The peripheral V1 domain, a 500-kDa complex responsible for ATP hydrolysis, contains at least eight different subunits of molecular weight 70-13 (subunits A-H). The integral V0 domain, a 250-kDa complex, functions in proton translocation and contains at least five different subunits of molecular weight 100-17 (subunits a-d). Biochemical and genetic analysis has been used to identify subunits and residues involved in nucleotide binding and hydrolysis, proton translocation, and coupling of these activities. Several mechanisms have been implicated in the regulation of vacuolar acidification in vivo, including control of pump density, regulation of assembly of V1 and V0 domains, disulfide bond formation, activator or inhibitor proteins, and regulation of counterion conductance. Recent information concerning targeting and regulation of V-ATPases has also been obtained.
液泡型（H⁺）-ATP酶（即V-ATP酶）在真核细胞内细胞器的酸化过程中发挥作用。V-ATP酶是由两个功能结构域组成的多亚基复合物。外周的V1结构域是一个负责ATP水解的500 kDa复合物，包含至少8种分子量为70 - 13 kDa的不同亚基（亚基A - H）。整合的V0结构域是一个250 kDa复合物，在质子转运中起作用，包含至少5种分子量为100 - 17 kDa的不同亚基（亚基a - d）。生化和遗传分析已被用于鉴定参与核苷酸结合与水解、质子转运以及这些活动偶联的亚基和残基。体内液泡酸化的调控涉及多种机制，包括泵密度控制、V1和V0结构域组装调控、二硫键形成、激活剂或抑制剂蛋白以及抗衡离子电导调控。最近也获得了有关V-ATP酶靶向和调控的信息。
