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APC2 associates with the actin cortex through a multipart mechanism to regulate cortical actin organization and dynamics in the Drosophila ovary
Author(s) -
MolinarInglis Olivia,
Oliver Stacie L.,
Rudich Paige,
Kunttas Ezgi,
McCartney Brooke M.
Publication year - 2018
Publication title -
cytoskeleton
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.95
H-Index - 86
eISSN - 1949-3592
pISSN - 1949-3584
DOI - 10.1002/cm.21471
Subject(s) - biology , microbiology and biotechnology , cell cortex , cytokinesis , actin , cortex (anatomy) , ferm domain , morphogenesis , adenomatous polyposis coli , cytoskeleton , cell , cell division , membrane protein , neuroscience , genetics , integral membrane protein , cancer , gene , colorectal cancer , membrane
The actin cortex that lines the plasma membrane of most eukaryotic cells resists external mechanical forces and plays critical roles in a variety of cellular processes including morphogenesis, cytokinesis, and cell migration. Despite its ubiquity and significance, we understand relatively little about the composition, dynamics, and structure of the actin cortex. Adenomatous polyposis coli (APC) proteins regulate the actin and microtubule cytoskeletons through a variety of mechanisms, and in some contexts, APC proteins are cortically enriched. Here we show that APC2 regulates cortical actin dynamics in the follicular epithelium and the nurse cells of the Drosophila ovary and in addition affects the distribution of cortical actin at the apical side of the follicular epithelium. To understand how APC2 influences these properties of the actin cortex, we investigated the mechanisms controlling the cortical localization of APC2 in S2 cultured cells. We previously showed that the N‐terminal half of APC2 containing the Armadillo repeats and the C‐terminal 30 amino acids (C30) are together necessary and sufficient for APC2's cortical localization. Our work presented here supports a model that cortical localization of APC2 is governed in part by self‐association through the N‐terminal APC Self‐Association Domain (ASAD) and a highly conserved coiled‐coil within the C30 domain.