Assembly of model postsynaptic densities involves interactions auxiliary to stoichiometric binding.

ABSTRACT: The assembly of functional biomolecular condensates often involves liquid-liquid phase separation (LLPS) of proteins with multiple modular domains, which can be folded or conformationally disordered to various degrees. To understand the LLPS-driving domain-domain interactions, a fundamental question is how readily the interactions in the condensed phase can be inferred from interdomain interactions in dilute solutions. In particular, are the interactions leading to LLPS exclusively those underlying the formation of discrete interdomain complexes in homogeneous solutions? We address this question by developing a mean-field LLPS theory of two stoichiometrically constrained solute species. The theory is applied to the neuronal proteins SynGAP and PSD-95, whose complex coacervate serves as a r

SUBMITTER: Lin YH 

PROVIDER: S-EPMC8758407 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature