<i>folded gastrulation</i>, cell shape change and the control of myosin localization

Dawes-Hoang, Rachel E.; Parmar, Kush M.; Christiansen, Audrey E.; Phelps, Chris B.; Brand, Andrea H.; Wieschaus, Eric

doi:10.1242/dev.017343

Cited by 94 publications

(174 citation statements)

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“…RhoGEF2 is an essential regulator of Rho1 activity during many different stages of Drosophila development including cellularization (Barrett et al, 1997;Dawes-Hoang et al, 2005;Grosshans et al, 2005;Hä cker and Perrimon, 1998;Nikolaidou and Barrett, 2004;Padash Barmchi et al, 2005). However, little has been known about the events and factors that control RhoGEF2 localization and subsequent Rho1 activation at the furrow canal.…”

Section: Discussionmentioning

confidence: 99%

Localization of RhoGEF2 during Drosophila cellularization is developmentally controlled by slam

Wenzl

Yan

Laupsien

et al. 2010

Mechanisms of Development

102

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Essential for proper function of small GTPases of the Rho family, which control many aspects of cytoskeletal and membrane dynamics, is their temporal and spatial control by activating GDP exchange factors (GEFs) and deactivating GTPase-activating-proteins (GAPs). The regulatory mechanisms controlling these factors are not well understood, especially during development, when the organization and behaviour of cells change in a stage dependent manner. During Drosophila cellularization Rho signalling and RhoGEF2 are involved in furrow canal formation and the organization of actin and myosin. Here we analyze, how RhoGEF2 is localized at the sites of membrane invagination. We show that the PDZ domain is necessary for localization and function of RhoGEF2 and identify Slam as a factor that is necessary for RhoGEF2 localization. We also demonstrate that Slam can recruit RhoGEF2 to ectopic sites. Furthermore we find that the PDZ domain of RhoGEF2 can form a complex with Slam invivo and that Slam transcripts and protein colocalize at the furrow canal and in basal particles. Based on these findings, we propose that accumulation of slam mRNA and protein at the presumptive invagination site provides a spatial and temporal trigger for RhoGEF2-Rho1 signalling.

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Section: Discussionmentioning

confidence: 99%

Localization of RhoGEF2 during Drosophila cellularization is developmentally controlled by slam

Wenzl

Yan

Laupsien

et al. 2010

Mechanisms of Development

102

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“…However, perhaps more convincing is the observed abrogation of CCC adhesive function by disruption of the circumferential cortical actin filament network but not by disruption of actin stress fibers or microtubules [53]. Moreover, a direct link between the CCC and actomyosin is required for particular morphogenetic changes during which active changes in cell shape occur in the presence of continued cell-cell adhesion [54]. As aE-catenin has been shown to bind to several other junction-associated, actin-binding protein partners, including ZO-1, spectrin, vinculin, a-actinin, vezatin, and the nectin-afadin complex (see also below), these molecular interactions might be responsible for the link of F-actin to cell junctions (reviewed in [44,55]).…”

Section: Present Models For the E-cadherin-catenin-cytoskeleton Intermentioning

confidence: 99%

The cell-cell adhesion molecule E-cadherin

Roy

Berx

2008

Cell. Mol. Life Sci.

1,098

808

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This review is dedicated to E-cadherin, a calcium-dependent cell-cell adhesion molecule with pivotal roles in epithelial cell behavior, tissue formation, and suppression of cancer. As founder member of the cadherin superfamily, it has been extensively investigated. We summarize the structure and regulation of the E-cadherin gene and transcript. Models for E-cadherin-catenin complexes and cell junctions are presented. The structure of the E-cadherin protein is discussed in view of the diverse functions of this remarkable protein. Homophilic and heterophilic adhesion are compared, including the role of E-cadherin as a receptor for pathogens. The complex post-translational processing of E-cadherin is reviewed, as well as the many signaling activities. The role of E-cadherin in embryonic development and morphogenesis is discussed for several animal models. Finally, we review the multiple mechanisms that disrupt E-cadherin function in cancer: inactivating somatic and germline mutations, epigenetic silencing by DNA methylation and epithelial to mesenchymal transition-inducing transcription factors, and dysregulated protein processing.

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“…By promoting clustering of cells with identical phenotypes, cadherins play a crucial role in the elaboration of various tissues during embryogenesis [2] and in the maintenance of adult tissue architecture. VE-cadherin is crucial for the proper assembly of vascular structures and maintenance of vascular integrity [3].…”

Section: Introductionmentioning

confidence: 99%

Structure of artificial and natural VE-cadherinbased adherens junctions

Taveau

Dubois

Bihan

et al. 2008

Biochemical Society Transactions

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In vascular endothelium, adherens junctions between endothelial cells are composed of VE-cadherin (vascular endothelial cadherin), an adhesive receptor that is crucial for the proper assembly of vascular structures and the maintenance of vascular integrity. As a classical cadherin, VE-cadherin links endothelial cells together by homophilic interactions mediated by its extracellular part and associates intracellularly with the actin cytoskeleton via catenins. Although, from structural crystallographic data, a dimeric structure arranged in a trans orientation has emerged as a potential mechanism of cell-cell adhesion, the cadherin organization within adherens junctions remains controversial. Concerning VE-cadherin, its extracellular part possesses the capacity to self-associate in solution as hexamers consisting of three antiparallel cadherin dimers. VE-cadherin-based adherens junctions were reconstituted in vitro by assembly of a VE-cadherin EC (extracellular repeat) 1-EC4 hexamer at the surfaces of liposomes. The artificial adherens junctions revealed by cryoelectron microscopy appear as a two-dimensional self-assembly of hexameric structures. This cadherin organization is reminiscent of that found in native desmosomal junctions. Further structural studies performed on native VE-cadherin junctions would provide a better understanding of the cadherin organization within adherens junctions. Homophilic interactions between cadherins are strengthened intracellularly by connection to the actin cytoskeleton. Recently, we have discovered that annexin 2, an actin-binding protein connects the VE-cadherin-catenin complex to the actin cytoskeleton. This novel link is labile and promotes the endothelial cell switch from a quiescent to an angiogenic state.

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folded gastrulation, cell shape change and the control of myosin localization

Cited by 94 publications

References 0 publications

Localization of RhoGEF2 during Drosophila cellularization is developmentally controlled by slam

Localization of RhoGEF2 during Drosophila cellularization is developmentally controlled by slam

The cell-cell adhesion molecule E-cadherin

Structure of artificial and natural VE-cadherinbased adherens junctions

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