Download Adherens Junctions: from Molecular Mechanisms to Tissue by Tony J. C. Harris (auth.), Tony Harris (eds.) PDF

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

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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.

J Cell Biol 163:525–534. 200307111 Dickinson DJ, Nelson WJ, Weis WI (2011) A polarized epithelium organized by b- and α-catenin predates cadherin and metazoan origins. Science 331:1336–1339. 1199633 Drees F, Pokutta S, Yamada S, Nelson WJ, Weis WI (2005) α-catenin is a molecular switch that binds E-cadherin-β-catenin and regulates actin-filament assembly. Cell 123:903–915. 021 Eisenmann DM (2005) Wnt signaling. WormBook 25:1–17 Elledge HM, Kazmierczak P, Clark P, Joseph JS, Kolatkar A, Kuhn P, Müller U (2010) Structure of the N terminus of cadherin 23 reveals a new adhesion mechanism for a subset of cadherin superfamily members.

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).

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