Optimized PAR-2 RING dimerization mediates cooperative and selective membrane binding for robust cell polarity.

ABSTRACT: Cell polarity networks are defined by quantitative features of their constituent feedback circuits, which must be tuned to enable robust and stable polarization, while also ensuring that networks remain responsive to dynamically changing cellular states and/or spatial cues during development. Using the PAR polarity network as a model, we demonstrate that these features are enabled by the dimerization of the polarity protein PAR-2 via its N-terminal RING domain. Combining theory and experiment, we show that dimer affinity is optimized to achieve dynamic, selective, and cooperative binding of PAR-2 to the plasma membrane during polarization. Reducing dimerization compromises positive feedback and robustness of polarization. Conversely, enhanced dimerization renders the network less responsiv

SUBMITTER: Bland T 

PROVIDER: S-EPMC11294563 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature