Isocalmodulin binds to the extracellular site of the plasma membrane and causes an increase in intracellular calcium levels

Calmodulin (CaM) is a highly conserved intracellular calcium ion sensor. In plants, extracellular CaM also affects many physiological functions as a peptide signal, but its binding site outside the cytoplasm is still controversial.

In May 2009, the Lin Jinxing research group of the Institute of Botany, Chinese Academy of Sciences published an article in "JBC". The researchers used the CaM cross-linking QD system to detect the single molecule level of CaM binding sites on the surface of plant cells and found that QD-CaM can selectively It is bound to the extracellular space of the plasma membrane and further positioned by high-resolution transmission electron microscopy, which confirms that the extracellular CaM binding site does exist on the surface of the plant cell membrane, but there is no CaM binding site on the plant cell wall. This study provides strong evidence for the application of nanometer technology in plant cell research. In addition, the researchers also used microinjection, FRET, and non-invasive micro-testing (SIET) techniques to prove that extracellular CaM, after binding to its extracellular binding point, can cause the intracellular second messenger Ca2 + signal to be enhanced. These findings It shows that plant extracellular CaM can play the role of its signal peptide by mediating transmembrane signal.

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