2015/02/01 by Emanuel Reithmann, Louis Reese, Erwin Frey · 6 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Physics and Astronomy · #Actin #Biochemistry #Biology #Biophysics #Cell biology #Chemical physics #Chemistry #Computer science #Diffusion #Diffusion and Search Dynamics #Diffusion process #Microtubule #Microtubule and mitosis dynamics #Physics #Protein Structure and Dynamics #Protein filament #Substrate (aquarium) #Thermodynamics #cond-mat.stat-mech #physics.bio-ph #q-bio.SC
paper · pdf · doi:10.1016/j.bpj.2014.12.053
published in Biophysical Journal 108(4), 787-790 (Elsevier BV) · 13 pages, 7 figures
openalex publication_date 2015/02/01 · arxiv created 2015/03/03 · arxiv updated 2015/03/04 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/05
The functional relevance of regulating proteins is often limited to specific binding sites such as the ends of microtubules or actin-filaments. A localization of proteins on these functional sites is of great importance. We present a quantitative theory for a diffusion and capture process, where proteins diffuse on a filament and stop diffusing when reaching the filament's end. It is found that end-association after one-dimensional diffusion is the main source for tip-localization of such proteins. As a consequence, diffusion and capture is highly efficient in enhancing the reaction velocity of enzymatic reactions, where proteins and filament ends are to each other as enzyme and substrate. We show that the reaction velocity can effectively be described within a Michaelis-Menten framework. Together one-dimensional diffusion and capture beats the (three-dimensional) Smoluchowski diffusion limit for the rate of protein association to filament ends.