Seven-Pass Transmembrane Cadherin CELSRs, and Fat4 and Dchs1 Cadherins: From Planar Cell Polarity to Three-Dimensional Organ Architecture

Shi, Dongbo; Arata, Masaki; Usui, Tadao; Fujimori, Toshihiko; Uemura, Tadashi

doi:10.1007/978-4-431-56033-3_10

Cited by 4 publications

(5 citation statements)

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“…Dachsous (Ds) is an evolutionarily conserved atypical cadherin (Clark et al, 1995;Rock et al, 2005;Thomas and Strutt, 2012;Sharma and McNeill, 2013;Shi et al, 2016). In epithelial cells, Ds is localized at apical cell boundaries and binds to another atypical cadherin, Fat (Ft), in a heterophilic fashion (Strutt and Strutt, 2002;Ma et al, 2003;Matakatsu and Blair, 2004;Ishiuchi et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Difference in Dachsous Levels between Migrating Cells Coordinates the Direction of Collective Cell Migration

2017

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In contrast to extracellular chemotactic gradients, how cell-adhesion molecules contribute to directing cell migration remains more elusive. Here we studied the collective migration of Drosophila larval epidermal cells (LECs) along the anterior-posterior axis and propose a migrating cell group-autonomous mechanism in which an atypical cadherin Dachsous (Ds) plays a pivotal role. In each abdominal segment, the amount of Ds in each LEC varied along the axis of migration (Ds imbalance), which polarized Ds localization at cell boundaries. This Ds polarity was necessary for coordinating the migratory direction. Another atypical cadherin, Fat (Ft), and an unconventional myosin Dachs, both of which bind to Ds, also showed biased cell-boundary localizations, and both were required for the migration. Altogether, we propose that the Ds imbalance within the migrating tissue provides the directional cue and that this is decoded by Ds-Ft-mediated cell-cell contacts, which restricts lamellipodia formation to the posterior end of the cell.

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Section: Introductionmentioning

confidence: 99%

Difference in Dachsous Levels between Migrating Cells Coordinates the Direction of Collective Cell Migration

2017

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“…For example, in the oviduct, the axis of the epithelial PCP lies along the longitudinal axis of the oviduct, and the morphological polarities extend over multiple cells, such as the folded structure formed by the epithelial sheet, the elongation of the apical surface of MCCs, and the orientation of multicilia (Shi et al, 2014;Koyama et al, 2016;Koyama et al, 2019). PCP factors are proteins involved in regulating PCP that were initially identified by genetic screens performed in Drosophila melanogaster; many are conserved in vertebrates (Butler and Wallingford, 2017;Devenport 2014;Yang and Mlodzik, 2015;Hale and Strutt, 2015;Boutin et al, 2012;Shi et al, 2013;Shi et al, 2016a). These factors localize asymmetrically in each cell according to the tissue's polarity.…”

Section: Introductionmentioning

confidence: 99%

Celsr1 and CAMSAP3 differently regulate intercellular and intracellular cilia orientation in oviduct multiciliated cells

Usami

Arata

Shi

et al. 2020

Preprint

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SummaryThe molecular mechanisms by which cilia orientation is coordinated within and between multiciliated cells (MCCs) is not fully understood. By observing the orientation of basal bodies (BB) in MCCs of mouse oviducts, here, we show that Celsr1, a planar cell polarity (PCP) factor involved in tissue polarity regulation, is dispensable for determining BB orientation in individual cells, whereas CAMSAP3, a microtubule minus-end regulator, is critical for this process but not for PCP. MCCs exhibit a characteristic BB orientation and microtubule gradient along the tissue axis, and these intracellular polarities were maintained in the cells lacking Celsr1, although the intercellular coordination of the polarities was partly disrupted. On the other hand, CAMSAP3 regulated the assembly of microtubules interconnecting BBs by localizing at the BBs, and its mutation led to disruption of intracellular coordination of BB orientation, but not affecting PCP factor localization. Thus, both Celsr1 and CAMSAP3 are responsible for BB orientation but in distinct ways; and therefore, their cooperation should be critical for generating functional multiciliated tissues.

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“…Cadherin EGF LAG seven-pass G-type receptors (CELSR) cadherins in vertebrates are homologous, referred to as Flamingo or Starry night, in flies ( 28 – 32 ). These seven-path transmembrane cadherins are classified within the adhesion G-protein-coupled receptors (GPCRs) ( 33 ).…”

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confidence: 99%

“…The mutual binding of CELSR cadherins is crucial for the asymmetric recruitment of specific molecules at the cell–cell interface in planar cell polarity, which leads to proper cell patterning. This is necessary for the formation of cilia and regular and polarity-dependent tissues ( 32 , 35 – 39 ). Cell aggregation assays and ex vivo analyses of brain slice cultures in previous studies show that cadherin ectodomains of CELSR2 can maintain cell aggregation and responsiveness of cell–cell contact for the upkeep of dendritic branches ( 40 ).…”

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“…Cell aggregation assays and ex vivo analyses of brain slice cultures in previous studies show that cadherin ectodomains of CELSR2 can maintain cell aggregation and responsiveness of cell–cell contact for the upkeep of dendritic branches ( 40 ). However, fundamental structural information regarding the binding mode of CELSR cadherins is lacking ( 32 , 34 , 41 ). Structural analysis of CELSR cadherins may provide insight into the physiological roles and diversification of binding modes of cadherin superfamily.…”

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Antiparallel dimer structure of CELSR cadherin in solution revealed by high-speed atomic force microscopy

Nishiguchi

Kasai

Uchihashi

2023

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

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Cadherin EGF LAG seven-pass G-type receptors (CELSR) cadherins, members of the cadherin superfamily, and adhesion G-protein-coupled receptors, play a vital role in cell–cell adhesion. The mutual binding of the extracellular domains (ectodomains) of CELSR cadherins between cells is crucial for tissue formation, including the establishment of planar cell polarity, which directs the proper patterning of cells. CELSR cadherins possess nine cadherin ectodomains (EC1–EC9) and noncadherin ectodomains. However, the structural and functional mechanisms of the binding mode of CELSR cadherins have not been determined. In this study, we investigated the binding mode of CELSR cadherins using single-molecule fluorescence microscopy, high-speed atomic force microscopy (HS-AFM), and bead aggregation assay. The fluorescence microscopy analysis results indicated that the trans -dimer of the CELSR cadherin constitutes the essential adhesive unit between cells. HS-AFM analysis and bead aggregation assay results demonstrated that EC1–EC8 entirely overlap and twist to form antiparallel dimer conformations and that the binding of EC1–EC4 is sufficient to sustain bead aggregation. The interaction mechanism of CELSR cadherin may elucidate the variation of the binding mechanism within the cadherin superfamily and physiological role of CELSR cadherins in relation to planar cell polarity.

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Seven-Pass Transmembrane Cadherin CELSRs, and Fat4 and Dchs1 Cadherins: From Planar Cell Polarity to Three-Dimensional Organ Architecture

Cited by 4 publications

References 126 publications

Difference in Dachsous Levels between Migrating Cells Coordinates the Direction of Collective Cell Migration

Difference in Dachsous Levels between Migrating Cells Coordinates the Direction of Collective Cell Migration

Celsr1 and CAMSAP3 differently regulate intercellular and intracellular cilia orientation in oviduct multiciliated cells

Antiparallel dimer structure of CELSR cadherin in solution revealed by high-speed atomic force microscopy

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