Department of Biological Science, Graduate School of Science, Hiroshima University, Kagamiyama, Higashi-Hiroshima, Japan.
Plant Signal Behav. 2011 Jul;6(7):924-6. doi: 10.4161/psb.6.7.15604.
Ca2+-dependent protein kinases (CDPKs) are encoded by a multigene family and are thought to play central roles in Ca2+ signaling in plants. Although the primary structures of CDPK isoforms are highly conserved, several studies suggested a distinct physiological function for each CDPK isoform in plants. Hence, there should be mechanisms by which individual CDPK specifically recognizes its substrate. Recently, the variable N-terminal domain of NtCDPK1 was shown to play an essential role in the specific recognition of the substrate. Because the variable N-terminal domain of other CDPKs may also be involved in the substrate recognition, the search for interacting proteins of the variable N-terminal domain would provide important clues to identify the physiological substrates of each CDPK. Additionally, manipulation of the variable N-terminal domain may enable us to engineer the substrate specificity of CDPK, leading a rational rewiring of cellular signaling pathways.
钙依赖蛋白激酶（CDPKs）是由多基因家族编码的，被认为在植物的钙信号转导中发挥核心作用。尽管 CDPK 同工型的一级结构高度保守，但有几项研究表明，每种 CDPK 同工型在植物中都具有独特的生理功能。因此，应该存在某种机制，使每个 CDPK 同工型能够特异性地识别其底物。最近，发现 NtCDPK1 的可变 N 端结构域在底物的特异性识别中发挥着重要作用。由于其他 CDPK 的可变 N 端结构域也可能参与底物识别，因此搜索可变 N 端结构域的相互作用蛋白将为鉴定每个 CDPK 的生理底物提供重要线索。此外，对可变 N 端结构域的操作可以使我们能够对 CDPK 的底物特异性进行工程改造，从而实现对细胞信号通路的合理重布线。
