By Tony J. C. Harris (auth.), Tony Harris (eds.)
Cell–cell adhesion is prime for the improvement and homeostasis of animal tissues and organs. Adherens junctions (AJs) are the simplest understood cell-cell adhesion complexes. during this quantity, a bunch of the world over well-known specialists experiences AJ biology over a variety of association; from atoms to molecules, to protein complexes, molecular networks, cells, tissues, and total animal improvement. AJs have additionally been a vital part of animal evolution, and play significant roles in melanoma improvement, pathogen an infection and different ailments. This e-book addresses significant questions encompassing AJ biology.
• How did AJs evolve?
• How do cadherins and catenins have interaction to gather AJs and mediate adhesion?
• How do AJs interface with different mobile equipment to couple adhesion with the total cellphone?
• How do AJs have an effect on telephone behaviour and multicellular improvement?
• How can irregular AJ task result in disease?
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Additional info for Adherens Junctions: from Molecular Mechanisms to Tissue Development and Disease
B The domain structures of AmqCadherin1, a classical cadherin-like protein from A. queenslandica, and MBCDH21, a cadherin with EGF and LmG in M. breviollis. c A comparison of the domain structures of β-catenin in the mouse and a β-catenin homolog in D. discoideum, Aardvark (adapted from Dickinson et al. 2011). d A comparison of the domain structures of αE-catenin and vinculin in the mouse and an α-catenin homolog in D. discoideum. (adapted from Dickinson et al. 2011) 2 Evolution of the Cadherin–Catenin Complex 27 ited.
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2001; Taveau et al. 2008). However, when VE-cadherin EC1-5 domains were produced using mammalian cell expression system, N-glycosylated recombinant proteins did not 3 The Three-Dimensional Structure of the Cadherin–Catenin Complex 45 hexamerize, but instead formed strand-swap dimers in solution (Brasch et al. 2011), suggesting that the glycosyl moieties block the surface patches involved in the trimer/hexamer formation observed in vitro. Second, a non-adhesive nascent cadherin molecule contains an N-terminal prodomain (residues 1–156 in mouse E-cadherin) (Takeichi 1988), which is cleaved by furin and other proprotein convertases in the trans-Golgi network to present the Asp-Trp pair as the first two residues of the EC1 domain (Ozawa and Kemler 1990; Stemmler 2008).