Regulation of cofilin phosphorylation and asymmetry in collective cell migration during morphogenesis

Zhang, Lijun; Luo, Jun; Wan, Ping; Wu, Jing; Laski, Frank A.; Chen, Jiong

doi:10.1242/dev.046870

Cited by 58 publications

(65 citation statements)

References 32 publications

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“…Because Ssh directly activates Cofilin through dephosphorylation, we first examined whether increased phospho-Cofilin (P-Cofilin) signal was detectable in the axons of the ssh 1-63 clone. We used a P-Cofilin antibody (Zhang et al, 2011) and detected a broad increase in the P-Cofilin signal (Fig. 5A″, red outline) in the ssh 1-63 mutant axons compared with the internal control axons (Fig.…”

Section: N17mentioning

confidence: 99%

The NAV2 homolog Sickie regulates F-actin-mediated axonal growth inDrosophilamushroom body neurons via the non-canonical Rac-Cofilin pathway

et al. 2014

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The Rac-Cofilin pathway is essential for cytoskeletal remodeling to control axonal development. Rac signals through the canonical RacPak-LIMK pathway to suppress Cofilin-dependent axonal growth and through a Pak-independent non-canonical pathway to promote outgrowth. Whether this non-canonical pathway converges to promote Cofilin-dependent F-actin reorganization in axonal growth remains elusive. We demonstrate that Sickie, a homolog of the human microtubule-associated protein neuron navigator 2, cellautonomously regulates axonal growth of Drosophila mushroom body (MB) neurons via the non-canonical pathway. Sickie was prominently expressed in the newborn F-actin-rich axons of MB neurons. A sickie mutant exhibited axonal growth defects, and its phenotypes were rescued by exogenous expression of Sickie. We observed phenotypic similarities and genetic interactions among sickie and Rac-Cofilin signaling components. Using the MARCM technique, distinct F-actin and phospho-Cofilin patterns were detected in developing axons mutant for sickie and Rac-Cofilin signaling regulators. The upregulation of Cofilin function alleviated the axonal defect of the sickie mutant. Epistasis analyses revealed that Sickie suppresses the LIMK overexpression phenotype and is required for Pak-independent Rac1 and Slingshot phosphatase to counteract LIMK. We propose that Sickie regulates F-actin-mediated axonal growth via the non-canonical Rac-Cofilin pathway in a Slingshot-dependent manner.

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Section: N17mentioning

confidence: 99%

The NAV2 homolog Sickie regulates F-actin-mediated axonal growth inDrosophilamushroom body neurons via the non-canonical Rac-Cofilin pathway

et al. 2014

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“…Twinstar encodes the only Drosophila homolog of Cofilin (Chen et al, 2001), an actin-binding protein, actindepolymerizing activity of which is inhibited through phosphorylation by LIM-kinase, which, in turn, is regulated by ROCK/Rok (Maekawa et al, 1999). Mutations in tsr have been shown to affect border cell migration and planar cell polarity in Drosophila (Blair et al, 2006;Zhang et al, 2011 ) that was shown previously to have no effect on salivary gland development on its own (Chandrasekaran and Beckendorf, 2005). Loss of tsr function in Rho1 1B homozygous embryos significantly suppressed the cell rearrangement and apical domain elongation defects of Rho1 1B mutant glands, which, in turn, narrowed the expanded lumens (Fig.…”

Section: Rho1mentioning

confidence: 99%

Rho GTPase controls Drosophila salivary gland lumen size through regulation of the actin cytoskeleton and Moesin

Bagumian

Galiano

et al. 2011

Development

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SUMMARYGeneration and maintenance of proper lumen size is important for tubular organ function. We report on a novel role for the Drosophila Rho1 GTPase in control of salivary gland lumen size through regulation of cell rearrangement, apical domain elongation and cell shape change. We show that Rho1 controls cell rearrangement and apical domain elongation by promoting actin polymerization and regulating F-actin distribution at the apical and basolateral membranes through Rho kinase. Loss of Rho1 resulted in reduction of F-actin at the basolateral membrane and enrichment of apical F-actin, the latter accompanied by enrichment of apical phosphorylated Moesin. Reducing cofilin levels in Rho1 mutant salivary gland cells restored proper distribution of F-actin and phosphorylated Moesin and rescued the cell rearrangement and apical domain elongation defects of Rho1 mutant glands. In support of a role for Rho1-dependent actin polymerization in regulation of gland lumen size, loss of profilin phenocopied the Rho1 lumen size defects to a large extent. We also show that Ribbon, a BTB domain-containing transcription factor functions with Rho1 in limiting apical phosphorylated Moesin for apical domain elongation. Our studies reveal a novel mechanism for controlling salivary gland lumen size, namely through Rho1-dependent actin polymerization and distribution and downregulation of apical phosphorylated Moesin.

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“…Our previous studies showed that cofilin is genetically required for cell migration in the Drosophila ovary and that it promotes lamellipodial protrusions (Chen et al, 2001;Zhang et al, 2011). Other genetic studies have shown that cofilin is essential for a variety of cellular and developmental processes requiring strong actin dynamics, including cytokinesis, axon growth and endocytosis (Bamburg, 1999;Ono, 2003).…”

Section: Introductionmentioning

confidence: 99%

AIP1 acts with cofilin to control actin dynamics during epithelial morphogenesis

et al. 2012

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SUMMARYDuring epithelial morphogenesis, cells not only maintain tight adhesion for epithelial integrity but also allow dynamic intercellular movement to take place within cell sheets. How these seemingly opposing processes are coordinated is not well understood. Here, we report that the actin disassembly factors AIP1 and cofilin are required for remodeling of adherens junctions (AJs) during ommatidial precluster formation in Drosophila eye epithelium, a highly stereotyped cell rearrangement process which we describe in detail in our live imaging study. AIP1 is enriched together with F-actin in the apical region of preclusters, whereas cofilin displays a diffuse and uniform localization pattern. Cofilin overexpression completely rescues AJ remodeling defects caused by AIP1 loss of function, and cofilin physically interacts with AIP1. Pharmacological reduction of actin turnover results in similar AJ remodeling defects and decreased turnover of E-cadherin, which also results from AIP1 deficiency, whereas an F-actin-destabilizing drug affects AJ maintenance and epithelial integrity. Together with other data on actin polymerization, our results suggest that AIP1 enhances cofilin-mediated actin disassembly in the apical region of precluster cells to promote remodeling of AJs and thus intercellular movement, but also that robust actin polymerization promotes AJ general adhesion and integrity during the remodeling process.

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Regulation of cofilin phosphorylation and asymmetry in collective cell migration during morphogenesis

Cited by 58 publications

References 32 publications

The NAV2 homolog Sickie regulates F-actin-mediated axonal growth inDrosophilamushroom body neurons via the non-canonical Rac-Cofilin pathway

The NAV2 homolog Sickie regulates F-actin-mediated axonal growth inDrosophilamushroom body neurons via the non-canonical Rac-Cofilin pathway

Rho GTPase controls Drosophila salivary gland lumen size through regulation of the actin cytoskeleton and Moesin

AIP1 acts with cofilin to control actin dynamics during epithelial morphogenesis

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