A role for Rho GTPases and cell–cell adhesion in single-cell motility in vivo

Kardash, Elena; Reichman-Fried, Michal; Maître, Jean-Léon; Boldajipour, Bijan; Papusheva, Ekaterina; Messerschmidt, Esther-Maria; Heisenberg, Carl‐Philipp; Raz, Erez

doi:10.1038/ncb2003

Cited by 242 publications

(292 citation statements)

References 39 publications

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“…Similar to our observations on presomitic mesoderm, the motility of chemokine-guided germ cells in zebrafish requires cadherins and the non-canonical planar polarity genes RhoA and Rac1 GTPases (Ueno and Greene, 2003;Kardash et al, 2010). In zebrafish, Wnt11 via Disheveled signals RhoA and Rho kinase to mediate convergence and extension (Marlow et al, 2002;Solnica-Krezel and Eaton, 2003).…”

Section: Developmental Dynamicssupporting

confidence: 82%

Cdc42 GTPase and Rac1 GTPase act downstream of p120 catenin and require GTP exchange during gastrulation of zebrafish mesoderm

Hsu

Muerdter

Knickerbocker

et al. 2012

Developmental Dynamics

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Background: We investigated the roles of p120 catenin, Cdc42, Rac1, and RhoA GTPases in regulating migration of presomitic mesoderm cells in zebrafish embryos. p120 catenin has dual roles: It binds the intracellular and juxtamembrane region of cadherins to stabilize cadherin-mediated adhesion with the aid of RhoA GTPase, and it activates Cdc42 GTPase and Rac1 GTPase in the cytosol to initiate cell motility. Results: During gastrulation of zebrafish embryos, knockdown of the synthesis of zygotic p120 catenind1 mRNAs with a splice-site morpholino caused lateral widening and anterior-posterior shortening of the presomitic mesoderm and somites and a shortened anterior-posterior axis. These phenotypes indicate a cell-migration effect. Co-injection of low amounts of wild-type Cdc42 or wild-type Rac1 or dominant-negative RhoA mRNAs, but not constitutively-active Cdc42 mRNA, rescued these p120 catenin d1-depleted embryos. Conclusions: These downstream small GTPases require appropriate spatiotemporal stimulation or cycling of GTP to guide mesodermal cell migration. A delicate balance of Rho GTPases and p120 catenin underlies normal development. Developmental Dynamics 241:1545-1561, 2012. V C 2012 Wiley Periodicals Inc.Key words: p120 Catenin (CTNND1); ARVCF; Delta-catenin (CTNND2b); Cdc42 GTPase; Rac1 GTPase, RhoA GTPase; gastrulation; presomitic mesoderm; somites; zebrafish Key findings p120 catetin is required for extension of the dorsal axis and normal migration of the presomitic mesoderm. Cdc42 and Rac1 GTPases are downstream of p120 catenin d1 signaling and require exchange of GTP for GDP. Local stimulation of the exchange of GTP for GDP in Cdc42 and Rac GTPases mediates directional migration of the presomitic mesoderm. A balance of the amount of p120 catenin d1 and localized activation or turnover of Cdc42, Rac1, and Rho GTPase are required for normal zebrafish cell migration. Accepted 31 July 2012 Developmental DynamicsABBREVIATIONS Ab antibody ARVCF armadillo repeat gene deleted in velo-cardio-facial syndrome CA constitutively active Chr chromosome C(t) relative amount of RT-PCR product hpf hours post-fertilization DN dominant negative d1 splice-MO antisense morpholino oligonucleotide to the 12 th splice site of zebrafish p120 catenin d1 p120 catenin d1 (CTNND1) also called p120 catenin, Xenopus p120 catenin is a CTNND1 p120 catenin d2b (CTNND2b) also called Delta-catenin Rok1 Rho kinase1 RT reverse transcriptase minus-RT controls without reverse transcriptase qRT-PCR quantitative real-time PCR WT wild-type Xp120 catenin mRNA Xenopus p120 catenin d1 mRNA.Additional Supporting Information may be found in the online version of this article.

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Section: Developmental Dynamicssupporting

confidence: 82%

Cdc42 GTPase and Rac1 GTPase act downstream of p120 catenin and require GTP exchange during gastrulation of zebrafish mesoderm

Hsu

Muerdter

Knickerbocker

et al. 2012

Developmental Dynamics

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“…2B). Thus, whereas shortly after their formation the PGCs can polarize and form structures that normally function in promoting their migration (22), they are initially immotile and express high levels of E-cadherin (9). The gradual decrease in rgs14a RNA expression level observed in the course of the transition from stationary to motile behavior is consistent with the idea that the Rgs14a protein plays a role in regulating the process.…”

Section: Significancesupporting

confidence: 71%

Temporal control over the initiation of cell motility by a regulator of G-protein signaling

Hartwig

Tarbashevich

Seggewiß³

et al. 2014

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

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The control over the acquisition of cell motility is central for a variety of biological processes in development, homeostasis, and disease. An attractive in vivo model for investigating the regulation of migration initiation is that of primordial germ cells (PGCs) in zebrafish embryos. In this study, we show that, following PGC specification, the cells can polarize but do not migrate before the time chemokine-encoded directional cues are established. We found that the regulator of G-protein signaling 14a protein, whose RNA is a newly identified germ plasm component, regulates the temporal relations between the appearance of the guidance molecules and the acquisition of cellular motility by regulating E-cadherin levels.rgs protein | cell adhesion

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“…The strengthening of cadherin-mediated intercellular adhesion has been attributed to several mechanisms, including GTPase activity (27)(28)(29)(30)(31), enhanced cadherin-cytoskeletal interactions (5,(32)(33)(34)(35), cadherin catch bonds (36), cadherin clustering (19,37,38), and altered cortical tension (5,6). Demonstrating that Colo 205 aggregation was caused by the allosteric regulation of E-cadherin required a demonstration that specific perturbations, which do not affect the binding site directly, caused quantitative changes in the E-cadherin affinity.…”

mentioning

confidence: 99%

Allosteric Regulation of E-Cadherin Adhesion

Shashikanth¹,

Petrova

Park³

et al. 2015

Journal of Biological Chemistry

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Background: Measured binding kinetics between Colo 205 cells tested the postulate that E-cadherin adhesion is allosterically regulated. Results: p120 catenin dephosphorylation or cell treatment with activating anti-E-cadherin antibody increased E-cadherin binding affinities by 2-3-fold. Conclusion: Perturbations that do not directly affect the binding site enhanced the adhesive function of E-cadherin. Significance: These biophysical measurements demonstrated that E-cadherin is allosterically regulated.

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A role for Rho GTPases and cell–cell adhesion in single-cell motility in vivo

Cited by 242 publications

References 39 publications

Cdc42 GTPase and Rac1 GTPase act downstream of p120 catenin and require GTP exchange during gastrulation of zebrafish mesoderm

Cdc42 GTPase and Rac1 GTPase act downstream of p120 catenin and require GTP exchange during gastrulation of zebrafish mesoderm

Temporal control over the initiation of cell motility by a regulator of G-protein signaling

Allosteric Regulation of E-Cadherin Adhesion

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