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  • Adherens Junctions/*physiology/ultrastructure  (1)
  • Arabidopsis/genetics/*metabolism/physiology  (1)
  • Nature Publishing Group (NPG)  (2)
  • American Association of Petroleum Geologists (AAPG)
  • Cambridge University Press
  • International Union of Crystallography (IUC)
  • Macmillian Magazines Ltd.
  • Royal Society
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  • Nature Publishing Group (NPG)  (2)
  • American Association of Petroleum Geologists (AAPG)
  • Cambridge University Press
  • International Union of Crystallography (IUC)
  • Macmillian Magazines Ltd.
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  • 1
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    Differential positioning of adherens junctions is associated with initiation of epithelial folding (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-03-30
    Description: During tissue morphogenesis, simple epithelial sheets undergo folding to form complex structures. The prevailing model underlying epithelial folding involves cell shape changes driven by myosin-dependent apical constriction. Here we describe an alternative mechanism that requires differential positioning of adherens junctions controlled by modulation of epithelial apical-basal polarity. Using live embryo imaging, we show that before the initiation of dorsal transverse folds during Drosophila gastrulation, adherens junctions shift basally in the initiating cells, but maintain their original subapical positioning in the neighbouring cells. Junctional positioning in the dorsal epithelium depends on the polarity proteins Bazooka and Par-1. In particular, the basal shift that occurs in the initiating cells is associated with a progressive decrease in Par-1 levels. We show that uniform reduction of the activity of Bazooka or Par-1 results in uniform apical or lateral positioning of junctions and in each case dorsal fold initiation is abolished. In addition, an increase in the Bazooka/Par-1 ratio causes formation of ectopic dorsal folds. The basal shift of junctions not only alters the apical shape of the initiating cells, but also forces the lateral membrane of the adjacent cells to bend towards the initiating cells, thereby facilitating tissue deformation. Our data thus establish a direct link between modification of epithelial polarity and initiation of epithelial folding.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3597240/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3597240/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Yu-Chiun -- Khan, Zia -- Kaschube, Matthias -- Wieschaus, Eric F -- 5R37HD15587/HD/NICHD NIH HHS/ -- P50 GM071508/GM/NIGMS NIH HHS/ -- R37 HD015587/HD/NICHD NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2012 Mar 28;484(7394):390-3. doi: 10.1038/nature10938.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22456706" target="_blank"〉PubMed〈/a〉
    Keywords: Adherens Junctions/*physiology/ultrastructure ; Animals ; *Cell Polarity ; Cell Shape ; Choristoma ; Drosophila Proteins/deficiency/genetics/metabolism ; Drosophila melanogaster/*cytology/*embryology/genetics/metabolism ; Epithelial Cells/*cytology/metabolism/ultrastructure ; Epithelium/*embryology/metabolism/ultrastructure ; Gastrula/cytology/embryology/metabolism/ultrastructure ; Gastrulation/*physiology ; Glycogen Synthase Kinase 3 ; Intracellular Signaling Peptides and Proteins/deficiency/genetics/metabolism ; Protein-Serine-Threonine Kinases/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    A receptor heteromer mediates the male perception of female attractants in plants (2016)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2016-02-11
    Description: Sexual reproduction requires recognition between the male and female gametes. In flowering plants, the immobile sperms are delivered to the ovule-enclosed female gametophyte by guided pollen tube growth. Although the female gametophyte-secreted peptides have been identified to be the chemotactic attractant to the pollen tube, the male receptor(s) is still unknown. Here we identify a cell-surface receptor heteromer, MDIS1-MIK, on the pollen tube that perceives female attractant LURE1 in Arabidopsis thaliana. MDIS1, MIK1 and MIK2 are plasma-membrane-localized receptor-like kinases with extracellular leucine-rich repeats and an intracellular kinase domain. LURE1 specifically binds the extracellular domains of MDIS1, MIK1 and MIK2, whereas mdis1 and mik1 mik2 mutant pollen tubes respond less sensitively to LURE1. Furthermore, LURE1 triggers dimerization of the receptors and activates the kinase activity of MIK1. Importantly, transformation of AtMDIS1 to the sister species Capsella rubella can partially break down the reproductive isolation barrier. Our findings reveal a new mechanism of the male perception of the female attracting signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Tong -- Liang, Liang -- Xue, Yong -- Jia, Peng-Fei -- Chen, Wei -- Zhang, Meng-Xia -- Wang, Ying-Chun -- Li, Hong-Ju -- Yang, Wei-Cai -- England -- Nature. 2016 Mar 10;531(7593):241-4. doi: 10.1038/nature16975. Epub 2016 Feb 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉State Key Laboratory of Molecular and Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China. ; University of Chinese Academy of Sciences, Beijing 100049, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26863186" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*metabolism/physiology ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Capsella/genetics/metabolism/physiology ; Cell Membrane/metabolism ; Mutation ; Ovule/metabolism ; Phenotype ; Phosphotransferases/chemistry/genetics/*metabolism ; Pollen Tube/genetics/growth & development/metabolism ; Protein Kinases/genetics/metabolism ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Reproduction ; *Signal Transduction
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
    Location Call Number Expected Availability
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    PAPER CURRENT
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