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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Intracellular calmodulin availability accessed with two-photon cross-correlation
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Intracellular calmodulin availability accessed with two-photon cross-correlation

机译：两光子互相关访问细胞内钙调蛋白的可用性

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摘要

The availability and interactions of signaling proteins are tightly regulated in time and space to produce specific and localized effects. For calmodulin (CaM), a key transducer of intracellular Ca~(2+) signaling, binding to its variety of targets initiates signaling cascades and regulates its subcellular localization, thereby making it unavailable for subsequent binding interactions. Among CaM's numerous targets, Ca~(2+) CaM-dependent protein kinase II is one of the most striking due to its unique ability to increase its affinity for CaM by autophosphorylation and to translocate when bound to Ca~(2+)/CaM. Two-photon fluorescence correlation spectroscopy and cross-correlation spectroscopy were utilized to compare mobility and molecular interactions between CaM and Ca~(2+)/CaM-depen-dent protein kinase II in solution and in living cells. These techniques revealed that CaM availability in cells could be altered by a change in intracellular conditions. Two-photon fluorescence cross-correlation spectroscopy exemplifies a generally applicable approach for studying protein-protein interactions in living cells that allows access to the behavior of signaling molecules within their native environment to probe for heterogeneities in signaling pathways in different cellular compartments.
机译：信号蛋白的可用性和相互作用在时间和空间上受到严格调节，以产生特定的局部效应。对于钙调蛋白（CaM），细胞内Ca〜（2+）信号传导的关键转换器，与其各种靶标结合会启动信号传导级联并调节其亚细胞定位，从而使其无法用于后续的结合相互作用。在CaM的众多靶标中，Ca〜（2+）CaM依赖性蛋白激酶II是最引人注目的之一，因为它具有通过自磷酸化增加对CaM的亲和力以及与Ca〜（2 +）/ CaM结合时易位的独特能力。 。利用双光子荧光相关光谱法和互相关光谱法比较了CaM和Ca〜（2 +）/ CaM依赖性蛋白激酶II在溶液和活细胞中的迁移率和分子相互作用。这些技术表明，细胞内CaM的可用性可通过细胞内条件的变化而改变。双光子荧光互相关光谱法是研究活细胞中蛋白质相互作用的一种普遍适用的方法，该方法允许访问其天然环境中信号分子的行为，以探测不同细胞区室中信号通路的异质性。

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