The Dictyostelium LvsA protein is localized on the contractile vacuole and is required for osmoregulation

The Dictyostelium LvsA protein is localized on the contractile vacuole and is required for osmoregulation
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DOI：
10.1034/j.1600-0854.2002.30107.x
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发表时间：
2002-01-01
期刊：
TRAFFIC
影响因子：
4.5
通讯作者：
De Lozanne, A
De Lozanne, A
中科院分区：
生物学2区
文献类型：
--
作者：
Gerald, NJ;Siano, M;De Lozanne, A

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LvsA是胞质分裂所必需的网骨藻蛋白，与哺乳动物beige/LYST蛋白家族相关。为了更好地了解这个新的蛋白质家族的功能，我们使用重组技术用GFP标记LvsA。GFP-LvsA主要与收缩空泡系统的膜相关，并且其在细胞质中也具有点状分布。两个标记的Dictyosteoblasticcractile空泡，空泡质子泵和钙调蛋白，显示广泛的共定位与GFP-LvsA的收缩空泡膜。有趣的是，LvsA与收缩液泡膜的关联仅发生在液泡的放电阶段。在LvsA突变体中，收缩液泡变得紊乱，钙调素从收缩液泡膜上解离。因此，收缩泡不能正常发挥功能，它可以膨胀，但似乎不能放电，LvsA突变体变得对ATP敏感。这些结果表明，LvsA可以与收缩泡膜室短暂的关联，这种关联是必要的收缩泡在ATP调节过程中的功能。这种与特定膜区室的短暂结合可能是其他含BEACH结构域蛋白的一般性质。
LvsA is a Dictyostelium protein that is essential for cytokinesis and that is related to the mammalian beige/LYST family of proteins. To better understand the function of this novel protein family we tagged LvsA with GFP using recombination techniques. GFP-LvsA is primarily associated with the membranes of the contractile vacuole system and it also has a punctate distribution in the cytoplasm. Two markers of the Dictyostelium contractile vacuole, the vacuolar proton pump and calmodulin, show extensive colocalization with GFP-LvsA on contractile vacuole membranes. Interestingly, the association of LvsA with contractile vacuole membranes occurs only during the discharge phase of the vacuole. In LvsA mutants the contractile vacuole becomes disorganized and calmodulin dissociates from the contractile vacuole membranes. Consequently, the contractile vacuole is unable to function normally, it can swell but seems unable to discharge and the LvsA mutants become osmosensitive, These results demonstrate that LvsA can associate transiently with the contractile vacuole membrane compartment and that this association is necessary for the function of the contractile vacuole during osmoregulation. This transient association with specific membrane compartments may be a general property of other BEACH-domain containing proteins.