posted on 2024-01-10, 17:39authored byWonhee
John Lee, Soo Jin Kim, Yongdeok Ahn, Jiseong Park, Siwoo Jin, Juhee Jang, Jinju Jeong, Minsoo Park, Young-Sam Lee, Junyeop Lee, Daeha Seo
Understanding the spatial organization
of membrane proteins is
crucial for unraveling key principles in cell biology. The reaction–diffusion
model is commonly used to understand biochemical patterning; however,
applying reaction–diffusion models to subcellular phenomena
is challenging because of the difficulty in measuring protein diffusivity
and interaction kinetics in the living cell. In this work, we investigated
the self-organization of the plasmalemma vesicle-associated protein
(PLVAP), which creates regular arrangements of fenestrated ultrastructures,
using single-molecule tracking. We demonstrated that the spatial organization
of the ultrastructures is associated with a decrease in the association
rate by actin destabilization. We also constructed a reaction–diffusion
model that accurately generates a hexagonal array with the same 130
nm spacing as the actual scale and informs the stoichiometry of the
ultrastructure, which can be discerned only through electron microscopy.
Through this study, we integrated single-molecule experiments and
reaction–diffusion modeling to surpass the limitations of static
imaging tools and proposed emergent properties of the PLVAP ultrastructure.