C-terminal phosphorylation modulates ERM-1 localization and dynamics to control cortical actin organization and support lumen formation during Caenorhabditiselegans development.

ABSTRACT: ERM proteins are conserved regulators of cortical membrane specialization that function as membrane-actin linkers and molecular hubs. The activity of ERM proteins requires a conformational switch from an inactive cytoplasmic form into an active membrane- and actin-bound form, which is thought to be mediated by sequential PIP₂ binding and phosphorylation of a conserved C-terminal threonine residue. Here, we use the single Caenorhabditiselegans ERM ortholog, ERM-1, to study the contribution of these regulatory events to ERM activity and tissue formation in vivo Using CRISPR/Cas9-generated erm-1 mutant alleles, we demonstrate that a PIP₂-binding site is crucially required for ERM-1 function. By contrast, dynamic regulation of C-terminal T544 p

SUBMITTER: Ramalho JJ 

PROVIDER: S-EPMC10755404 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature