Presentation Information
[C06-02]Reaction-diffusion modeling of protein domain formation on the endoplasmic reticulum in eukaryotic cells
*Tomoyo Nishigaki1, Masashi Tachikawa1 (1. Grad. Sch. of Nanobioscience, Yokohama City Univ. (Japan))
Keywords:
reaction-diffusion model,ER exit site (ERES),Sar1p,Sec23/24p,membrane traffic
Discovering the mechanism of membrane traffic, a system for transporting macromolecules such as proteins within the cell by wrapping them in a phospholipid membrane, has been one of the primary goals for researchers, as it is essential for understanding the structures of nervous system, immune system, and cancer development. In membrane traffic, transport vesicles assembled on the membrane of the source organelle bud off and fuse with the membrane of the destination organelle to deliver the molecules that form the transport vesicle and the macromolecules inside the transport vesicle. Transport between the endoplasmic reticulum (ER) as the source organelle and the Golgi apparatus as the destination organelle is one of the most explored pathways of membrane traffic. However, analytical research with mathematical models on the formation of ER exit site (ERES), the protein domain where transport vesicles are assembled, has not been conducted sufficiently. Thus, in this study, Sar1p and Sec23/24p, two main components of transport vesicles, were chosen to examine the formation process of ERES. To achieve this goal, mathematical models using reaction-diffusion equations were built, investigated, and evaluated based on prior studies. Model 1 suggested the stable accumulation of Sec23/24p molecules, but did not show the characteristics of Sar1p that previous research observed; while Model 2 showed the Sar1p characteristics yet failed to display the stable Sec23/24p accumulation.