Oligomerization and positive feedback on membrane recruitment encode dynamically stable PAR-3 asymmetries in the <i>C. elegans</i> zygote.

ABSTRACT: Studies of PAR polarity have emphasized a paradigm in which mutually antagonistic PAR proteins form complementary polar domains in response to transient cues. A growing body of work suggests that the oligomeric scaffold PAR-3 can form unipolar asymmetries without mutual antagonism, but how it does so is largely unknown. Here we combine single molecule analysis and modeling to show how the interplay of two positive feedback loops promotes dynamically stable unipolar PAR-3 asymmetries in early C. elegans embryos. First, the intrinsic dynamics of PAR-3 membrane binding and oligomerization encode negative feedback on PAR-3 dissociation. Second, membrane-bound PAR-3 promotes its own recruitment through a mechanism that requires the anterior polarity proteins PAR-6 and PKC-3. Using a kine

SUBMITTER: Lang CF 

PROVIDER: S-EPMC11383301 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature