Differential effects of G- and F-actin on the plasma membrane calcium pump activity.

Differential effects of G- and F-actin on the plasma membrane calcium pump activity.
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DOI:
10.1007/s12013-012-9467-6
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发表时间:
2013-05
影响因子:
2.6
通讯作者:
Rossi, Juan P. F. C.
Rossi, Juan P. F. C.
中科院分区:
生物学4区
文献类型:
--
作者:
Vanagas, Laura;Candelaria de La Fuente, Maria;Dalghi, Marianela;Ferreira-Gomes, Mariela;Rossi, Rolando C.;Strehler, Emanuel E.;Mangialavori, Irene C.;Rossi, Juan P. F. C.

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我们先前已经表明质膜钙ATP酶(PMCA)泵活性受膜蛋白浓度的影响(Vanagas等人,Biochim Biophys Acta 1768:1641-1644,2007)。结果表明,参与的肌动蛋白细胞骨架的证据。在这项研究中,我们探讨了肌动蛋白的聚合状态及其对纯化PMCA活性的影响之间的关系。我们的研究结果表明,PMCA协会与肌动蛋白细胞骨架,这种相互作用导致调制的催化活性,涉及磷酸化的中间泵。肌动蛋白聚合的状态决定了它是否作为泵的激活剂或抑制剂:G-肌动蛋白和/或短的寡聚体激活泵,而F-肌动蛋白抑制it. The肌动蛋白对PMCA的影响是直接相互作用的结果,证明了免疫印迹和共沉淀实验。两者合计,这些研究结果表明,与肌动蛋白的相互作用发挥了动态的作用,在调节PMCA介导的Ca 2+挤出通过膜。我们的研究结果提供了进一步的证据,作为许多细胞骨架相关的膜蛋白的特性的激活-抑制现象,其中细胞骨架不再限于机械功能,而是动态地参与调节与其相互作用的整合蛋白的活性。
We have previously shown that plasma membrane calcium ATPase (PMCA) pump activity is affected by the membrane protein concentration (Vanagas et al., Biochim Biophys Acta 1768:1641–1644, 2007). Results show evidences for the involvement of the actin cytoskeleton. In this study, we explored the relationship between the polymerization state of actin and its effects on purified PMCA activity. Our results show that PMCA associates with the actin cytoskeleton and this interaction causes a modulation of the catalytic activity involving the phosphorylated intermediate of the pump. The state of actin polymerization determines whether it acts as an activator or an inhibitor of the pump: G-actin and/or short oligomers activate the pump, while F-actin inhibits it. The effects of actin on PMCA are the consequence of direct interaction as demonstrated by immunoblotting and cosedimentation experiments. Taken together, these findings suggest that interactions with actin play a dynamic role in the regulation of PMCA-mediated Ca2+ extrusion through the membrane. Our results provide further evidence of the activation–inhibition phenomenon as a property of many cytoskeleton-associated membrane proteins where the cytoskeleton is no longer restricted to a mechanical function but is dynamically involved in modulating the activity of integral proteins with which it interacts.
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