Mechanical and kinetic factors drive sorting of F-actin cross-linkers on bundles.

ABSTRACT: In cells, actin-binding proteins (ABPs) sort to different regions to establish F-actin networks with diverse functions, including filopodia used for cell migration and contractile rings required for cell division. Recent experimental work uncovered a competition-based mechanism that may facilitate spatial localization of ABPs: binding of a short cross-linker protein to 2 actin filaments promotes the binding of other short cross-linkers and inhibits the binding of longer cross-linkers (and vice versa). We hypothesize this sorting arises because F-actin is semiflexible and cannot bend over short distances. We develop a mathematical theory and lattice models encompassing the most important physical parameters for this process and use coarse-grained simulations with explicit cross-linkers to c

SUBMITTER: Freedman SL 

PROVIDER: S-EPMC6697872 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature