A novel role for an APC2-Diaphanous complex in regulating actin organization in<i>Drosophila</i>

Webb, Rebecca L.; Zhou, Meng-Ning; McCartney, Brooke M.

doi:10.1242/dev.026963

Cited by 38 publications

(67 citation statements)

References 51 publications

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“…APC2 localizes with cortical actin throughout this actin cycle (McCartney et al, 1999), and APC2-null embryos exhibit defects in furrow extension (Fig. 8C,D) (Webb et al, 2009). To determine whether the cortical enrichment of APC2 is required for furrow extension, we first asked whether the C30 domain is required for the localization of APC2 to cortical actin in the 1595 The cellular functions of cortical APC2 (Fig.…”

Section: Cortical Enrichment Of Apc2 Is Required For Actin Pseudocleamentioning

confidence: 92%

“…8C,D). To quantify furrow extension defects from tangential sections, we determined the percentage of incomplete rings at four different depths as described previously (Webb et al, 2009) (supplementary material Fig. S3A).…”

Section: Cortical Enrichment Of Apc2 Is Required For Actin Pseudocleamentioning

confidence: 99%

“…We have shown previously that mutations in APC2 that disrupt cortical enrichment also disrupt destruction complex activity (McCartney et al, 2006). In addition, we have shown that APC2 together with the formin Diaphanous (Dia) promotes actin pseudocleavage furrow extension in the syncytial Drosophila embryo (Webb et al, 2009). Cortical enrichment of APC2 with actin plays a role in this process, as disruption of the cortical enrichment of APC2 by its mutation or by loss of Dia is correlated with furrow extension defects (Webb et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

“…In addition, we have shown that APC2 together with the formin Diaphanous (Dia) promotes actin pseudocleavage furrow extension in the syncytial Drosophila embryo (Webb et al, 2009). Cortical enrichment of APC2 with actin plays a role in this process, as disruption of the cortical enrichment of APC2 by its mutation or by loss of Dia is correlated with furrow extension defects (Webb et al, 2009). These findings suggest that cortical enrichment plays an important role in both the Wnt signaling and the cytoskeletal functions of APC2.…”

Section: Introductionmentioning

confidence: 99%

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Cortical localization of APC2 plays a role in actin organization but not in Wnt signaling inDrosophila

Zhou

Kunttas-Tatli

Zimmerman

et al. 2011

Journal of Cell Science

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SummaryThe tumor suppressor Adenomatous polyposis coli (APC) has roles in both Wnt signaling and in actin and microtubule organization. Within the cell, APC proteins have been reported to localize in the cytoplasm, at the cell cortex and in the nucleus. How these localizations relate to the functions of the protein is an aspect of APC biology that is poorly understood. Using Drosophila S2 cells, we have dissected the structural and functional requirements for the cortical localization of Drosophila APC2. Here, we show that both the Armadillo repeats and a novel C-terminal domain are necessary for the cortical localization of APC2 in S2 cells and in the embryo, and that neither domain alone is sufficient for this localization. Furthermore, we show that the Armadillo repeats mediate selfassociation of APC2 molecules. To test the function of the cortical localization of APC2, we asked whether an APC2 protein deleted for the C-terminal localization domain could rescue APC mutant defects in Wnt signaling and actin organization in the Drosophila embryo. We show that although cortical localization is required for the APC2 function in organizing actin, cortical localization is dispensable for its role in regulating Wnt signaling.

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Section: Cortical Enrichment Of Apc2 Is Required For Actin Pseudocleamentioning

confidence: 92%

Section: Cortical Enrichment Of Apc2 Is Required For Actin Pseudocleamentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Cortical localization of APC2 plays a role in actin organization but not in Wnt signaling inDrosophila

Zhou

Kunttas-Tatli

Zimmerman

et al. 2011

Journal of Cell Science

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“…Each appears to cooperate with its respective formin in assembling specific structures; Spire and Cappuccino are both required for proper assembly of an actin mesh in the course of oocyte development (47), whereas Bud6 augments actin cable assembly by Bni1 and APC interacts with Diaphanous to promote pseudocleavage furrow formation and extension in Drosophila embryos (48). Spire, Bud6, and APC each bind just C-terminal to the FH2 domain of their respective formin, likely blocking the actin-monomer binding ability of this portion of the formin but apparently superseding it functionally by contributing the ability to bind multiple actin monomers.…”

Section: Discussionmentioning

confidence: 99%

Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6

Graziano

Park

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Formin proteins and their associated factors cooperate to assemble unbranched actin filaments in diverse cellular structures. The Saccharomyces cerevisiae formin Bni1 and its associated nucleation-promoting factor (NPF) Bud6 generate actin cables and mediate polarized cell growth. Bud6 binds to both the tail of the formin and G-actin, thereby recruiting monomeric actin to the formin to create a nucleation seed. Here, we structurally and functionally dissect the nucleation-promoting C-terminal region of Bud6 into a Bni1-binding “core” domain and a G-actin binding “flank” domain. The ∼2-Å resolution crystal structure of the Bud6 core domain reveals an elongated dimeric rod with a unique fold resembling a triple-helical coiled-coil. Binding and actin-assembly assays show that conserved residues on the surface of this domain mediate binding to Bni1 and are required for NPF activity. We find that the Bni1 dimer binds two Bud6 dimers and that the Bud6 flank binds a single G-actin molecule. These findings suggest a model in which a Bni1/Bud6 complex with a 2:4 subunit stoichiometry assembles a nucleation seed with Bud6 coordinating up to four actin subunits.

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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

et al. 2018

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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.

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A novel role for an APC2-Diaphanous complex in regulating actin organization inDrosophila

Cited by 38 publications

References 51 publications

Cortical localization of APC2 plays a role in actin organization but not in Wnt signaling inDrosophila

Cortical localization of APC2 plays a role in actin organization but not in Wnt signaling inDrosophila

Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6

APC2 associates with the actin cortex through a multipart mechanism to regulate cortical actin organization and dynamics in the Drosophila ovary

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