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首页> 外文期刊>Cellular Signalling >The C1 and C2 domains target human type 6 adenylyl cyclase to lipid rafts and caveolae
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The C1 and C2 domains target human type 6 adenylyl cyclase to lipid rafts and caveolae

机译：C1和C2域将人6型腺苷酸环化酶靶向脂质筏和小窝

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Previous data has shown that adenylyl cyclase type 6 (AC6) is expressed principally in lipid rafts or caveolae of cardiac myocytes and other cell types while certain other isoforms of AC are excluded from these microdomains. The mechanism by which AC6 is localized to lipid rafts or caveolae is unknown. In this study, we show AC6 is localized in lipid rafts of COS-7 cells (expressing caveolin-1) and in HEK-293 cells or cardiac fibroblasts isolated from caveolin-1 knock-out mice (both of which lack prototypical caveolins). To determine the region of AC6 that confers raft localization, we independently expressed each of the major intracellular domains, the N-terminus, C1 and C2 domains, and examined their localization with various approaches. The N-terminus did not associate with lipid rafts or caveolae of either COS-7 or HEK-293 cells nor did it immunoprecipitate with caveolin-1 when expressed in COS-7 cells. By contrast, the C1 and C2 domains each associated with lipid rafts to varying degrees and were present in caveolin-1 immunoprecipitates. There were no differences in the pattern of localization of either the C1 or C2 domains between COS-7 and HEK-293 cells. Further dissection of the Cl domain into four individual proteins indicated that the N-terminal half of this domain is responsible for its raft localization. To probe for a role of a putative palmitoylation motif in the C-terminal portion of the C2 domain, we expressed various truncated forms of AC6 lacking most or all of the C-terminal 41 amino acids. These truncated AC6 proteins were not altered in terms of their localization in lipid rafts or their catalytic activity, implying that this C-terminal region is not required for lipid raft targeting of AC6. We conclude that while the C1 domain may be most important, both the C1 and C2 domains of AC6 play a role in targeting AC6 to lipid rafts. (c) 2008 Elsevier Inc. All rights reserved.
机译：先前的数据表明，腺苷酸环化酶6型（AC6）主要在心肌细胞和其他细胞类型的脂质筏或小窝中表达，而AC的某些其他亚型则从这些微区中排除。 AC6定位于脂质筏或小窝的机制尚不清楚。在这项研究中，我们显示AC6定位在COS-7细胞的脂质筏中（表达小窝蛋白1）和HEK-293细胞或从小窝蛋白1敲除小鼠中分离的心脏成纤维细胞（均缺乏原型小窝蛋白）。为了确定赋予筏定位的AC6区域，我们独立表达了每个主要的细胞内结构域，N末端，C1和C2结构域，并使用各种方法检查了它们的定位。 N末端不与COS-7或HEK-293细胞的脂筏或小窝相关，在COS-7细胞中表达时也不与小窝蛋白1免疫沉淀。相比之下，C1和C2域分别与脂质筏相关，程度不同，并存在于Caveolin-1免疫沉淀物中。 COS-7和HEK-293细胞之间C1或C2结构域的定位模式没有差异。将C1结构域进一步分解成四个单独的蛋白质，表明该结构域的N末端一半负责其筏的定位。为了探测在C2域的C端部分中假定的棕榈酰化基序的作用，我们表达了缺少大多数或全部C端41个氨基酸的各种截短形式的AC6。这些截短的AC6蛋白在脂质筏中的定位或催化活性方面均未改变，这意味着脂质筏靶向AC6不需要此C端区域。我们得出的结论是，尽管C1域可能是最重要的，但AC6的C1和C2域都在将AC6靶向脂质筏的过程中发挥了作用。 （c）2008 Elsevier Inc.保留所有权利。

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