Abstract
We investigate to clarify details of dynamic structure and function of Golgi complex in which locates in the center of membrane traffic. It was found that the secretory glycoprotein α-amlyase I-1 is transport to the plastid through the ER-Golgi system in rice non-secretory cells overexpressing the α-amlyase I-1, suggesting that the Golgi complex has a yet unknown sorting system. In the present communication, we described structural changes in Golgi membranes in the cells overexpressing glycoproteins. EM studies showed that number of the Golgi in transgenic cells was significantly increased in comparison with that in the wild-type. Cell fractionation studies employing a sucrose density gradient centrifugation-floating revealed that the density of the GNTI-associated Golgi membranes in cells overexpressing glycoproteins was markedly increased. It strongly suggests that the components of Golgi membranes are dynamically rearranged for responding to change of the Golgi function.
