Novel transport function of adherens junction revealed by live imaging in Drosophila

Li, Yu-Chiao; Yang, Wen‐Ting; Cheng, Linyi; Lin, Chiao-Ming; Ho, Yu-Huei; Lin, Pei-Yi; Chen, Bi-Chang; Rickoll, Wayne L.; Hsu, Jui-Chou

doi:10.1016/j.bbrc.2015.05.125

Cited by 5 publications

(2 citation statements)

References 22 publications

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“…AJs are a cell-cell adhesion device that plays a vital role during epithelial morphogenesis to maintain epithelial integrity in sensory organs, such as the chicken sensory organ [ 42 ], the lateral line of zebrafish [ 43 ], and the anterior sensory organ of Caenorhabditis elegans [ 44 ]. However, recent studies of Drosophila embryos revealed that AJs mediate intercellular movement of E-cadherin and epidermal growth factor receptor-containing vesicles [ 45 ]; thus, AJs mediate cell-to-cell signaling between adjacent epithelial cells, suggesting potential cell-to-cell signal transmission between the CBAS and the CB, as will be discussed later.…”

Section: Discussionmentioning

confidence: 99%

Immunohistochemical and ultrastructural properties of the larval ciliary band-associated strand in the sea urchin Hemicentrotus pulcherrimus

Katow

Yoshida

et al. 2016

Front Zool

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BackgroundThe swimming activity of sea urchin larvae is dependent on the ciliary band (CB) on the larval surface and is regulated by several neurotransmitters, including serotonin (5HT), dopamine, and γ-aminobutyric acid (GABA). However, the CB signal transmission mechanism remains unknown. The present study investigated the structural relationship between the CB and external signal receptors by immunohistochemical and transmission electron microscopic analyses of sea urchin, Hemicentrotus pulcherrimus, larvae.ResultsGlutamate decarboxylase (GAD; GABA synthetase) was detected in a strand of multiple cells along the circumoral CB in 6-arm plutei. The GAD-expressing strand was closely associated with the CB on the oral ectoderm side. The ciliary band-associated strand (CBAS) also expressed the 5HT receptor (5HThpr) and encephalopsin (ECPN) throughout the cytoplasm and comprised 1- to 2-μm diameter axon-like long stretched regions and sporadic 6- to 7-μm diameter bulbous nucleated regions (perikarya) that protruded into the oral ectoderm side. Besides the laterally polarized morphology of the CBAS cells, Epith-2, which is the epithelial lateral cell surface-specific protein of the sea urchin embryo and larva, was expressed exclusively by perikarya but not by the axon-like regions. The CBAS exposed its narrow apical surface on the larval epithelium between the CB and squamous cells and formed adherens junctions (AJs) on the apical side between them. Despite the presence of the CBAS axon-like regions, tubulins, such as α-, β-, and acetylated α-tubulins, were not detected. However, the neuroendocrine cell marker protein synaptophysin was detected in the axon-like regions and in bouton-like protrusions that contained numerous small ultrastructural vesicles.ConclusionsThe unique morphology of the CBAS in the sea urchin larva epithelium had not been reported. The CBAS expresses a remarkable number of receptors to environmental stimuli and proteins that are probably involved in signal transmission to the CB. The properties of the CBAS explain previous reports that larval swimming is triggered by environmental stimuli and suggest crosstalk among receptors and potential plural sensory functions of the CBAS.

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Section: Discussionmentioning

confidence: 99%

Immunohistochemical and ultrastructural properties of the larval ciliary band-associated strand in the sea urchin Hemicentrotus pulcherrimus

Katow

Yoshida

et al. 2016

Front Zool

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“…Ed has functional similarities to mammalian nectins: both are junctional components that belong to the Ig superfamily and recruit the F-actin binding protein Canoe (afadin in mammals); however, but as their domain structure differs, Ed is considered to be nectin like rather than a nectin ortholog ( Mandai et al, 2013 ; Wei et al, 2005 ). Ed has previously been observed to colocalise with early Rab5, late Rab7 and recycling Rab11 endosomal vesicles ( Fetting et al, 2009 ; Li et al, 2015 ; Rawlins et al, 2003a ). As Rab11 but not Rab5- or Rab7-positive vesicles accumulate in RASSF8 mutant clones ( Figs 3 and 4 ), we performed colocalisation analysis of Rab11 and Ed ( Fig.…”

Section: Resultsmentioning

confidence: 88%

RASSF8-mediated transport of Echinoid via the exocyst promotesDrosophilawing elongation and epithelial ordering

et al. 2021

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Cell-cell junctions are dynamic structures that maintain cell cohesion and shape in epithelial tissues. During development, junctions undergo extensive rearrangements to drive the epithelial remodelling required for morphogenesis. This is particularly evident during axis elongation, where neighbour exchanges, cell-cell rearrangements and oriented cell divisions lead to large-scale alterations in tissue shape. Polarised vesicle trafficking of junctional components by the exocyst complex has been proposed to promote junctional rearrangements during epithelial remodelling, but the receptors that allow exocyst docking to the target membranes remain poorly understood. Here, we show that the adherens junction component Ras Association domain family 8 (RASSF8) is required for the epithelial re-ordering that occurs during Drosophila pupal wing proximo-distal elongation. We identify the exocyst component Sec15 as a RASSF8 interactor. RASSF8 loss elicits cytoplasmic accumulation of Sec15 and Rab11-containing vesicles. These vesicles also contain the nectin-like homophilic adhesion molecule Echinoid, whose depletion phenocopies the wing elongation and epithelial packing defects observed in RASSF8 mutants. Thus, our results suggest that RASSF8 promotes exocyst-dependent docking of Echinoid-containing vesicles during morphogenesis.

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Adherens junction-associated pores mediate the intercellular transport of endosomes and cytoplasmic proteins

Yang

Lin

et al. 2018

Biochemical and Biophysical Research Communications

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Novel transport function of adherens junction revealed by live imaging in Drosophila

Cited by 5 publications

References 22 publications

Immunohistochemical and ultrastructural properties of the larval ciliary band-associated strand in the sea urchin Hemicentrotus pulcherrimus

Immunohistochemical and ultrastructural properties of the larval ciliary band-associated strand in the sea urchin Hemicentrotus pulcherrimus

RASSF8-mediated transport of Echinoid via the exocyst promotesDrosophilawing elongation and epithelial ordering

Adherens junction-associated pores mediate the intercellular transport of endosomes and cytoplasmic proteins

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