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首页> 外文期刊>Channels >Some assembly required: SOCE and Orai1 channels couple to NFAT transcriptional activity via calmodulin and calcineurin
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Some assembly required: SOCE and Orai1 channels couple to NFAT transcriptional activity via calmodulin and calcineurin

机译：需要一些组装：SOCE和Orai1通道通过钙调蛋白和钙调神经磷酸酶偶联至NFAT转录活性

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摘要

Advances in our ability to monitor the temporal and spatial dynamics of intracellular second messengers such as Ca~(2+) and cyclic nucleotides at millisecond and sub-micron levels of resolution have greatly increased our understanding of cellular signal transduction mechanisms. Thus, it is now well appreciated that second messengers can rise and fall within discrete regions of the intracellular compartment, as opposed to global changes, and on a time scale determined by the local collection of signaling molecules responsible for the synthesis and degradation/re-uptake of the second messenger. Efforts to identify the components of such macromolecular signaling domains have revealed the presence of hormone receptors, modifying enzymes and scaffolding proteins that tend to assemble and organize these complexes. Emerging evidence now suggests that these signal transduction entities need not be pre-existing, static complexes within the cell, but in fact, may dynamically assemble in response to a specific stimulus. Such an arrangement would thus allow key signaling molecules to be trafficked where they are needed, thereby allowing a cell to utilize these resources more effectively. On the flip side, having such molecules constantly remain within a single cellular domain would facilitate rapid signaling responses and help maintain fidelity of the pathway.
机译：我们在毫秒级和亚微米级的分辨率下监测细胞内第二信使（例如Ca〜（2+）和环状核苷酸）的时空动态的能力大大提高了我们对细胞信号转导机制的了解。因此，现已充分认识到，第二信使可以在细胞内区室的离散区域内上升和下降，这与全局变化相反，并且可以在时间范围内由负责合成和降解/重新构建的信号分子的局部集合确定。吸收第二个使者。鉴定此类大分子信号结构域的成分的努力揭示了激素受体，修饰酶和支架蛋白的存在，这些激素易于组装和组织这些复合物。现在有新的证据表明，这些信号转导实体不必是细胞内预先存在的静态复合物，但实际上，它们可以响应特定的刺激而动态组装。因此，这样的布置将允许关键信号分子被贩运到需要它们的地方，从而允许小区更有效地利用这些资源。另一方面，使这些分子恒定地保留在单个细胞结构域内将促进快速的信号反应并有助于维持该途径的保真度。

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