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 key for the advance and homeostasis of animal tissues and organs. Adherens junctions (AJs) are the easiest understood cell-cell adhesion complexes. during this quantity, a gaggle of the world over well-known specialists experiences AJ biology over quite a lot of association; from atoms to molecules, to protein complexes, molecular networks, cells, tissues, and total animal improvement. AJs have additionally been an essential component of animal evolution, and play principal 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 collect AJs and mediate adhesion?
• How do AJs interface with different mobile equipment to couple adhesion with the entire mobile?
• How do AJs impact phone behaviour and multicellular improvement?
• How can irregular AJ task bring about disease?

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Extra resources for Adherens Junctions: from Molecular Mechanisms to Tissue Development and Disease

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J Cell Biol 185:959–967. 200811030 32 H. Oda Iwai Y, Usui T, Hirano S, Steward R, Takeichi M, Uemura T (1997) Axon patterning requires DN-cadherin, a novel neuronal adhesion receptor, in the Drosophila embryonic CNS. Neuron 19:77–89. 1016/S0896-6273(00)80349-9 Kanno M, Isa Y, Aoyama Y, Yamamoto Y, Nagai M, Ozawa M, Kitajima Y (2008) p120-catenin is a novel desmoglein 3 interacting partner: identification of the p120-catenin association site of desmoglein 3. Exp Cell Res 314:1683–1692. 031 Kazmierczak P, Sakaguchi H, Tokita J, Wilson-Kubalek EM, Milligan RA, Müller U, Kachar B (2007) Cadherin 23 and protocadherin 15 interact to form tip-link filaments in sensory hair cells.

Genes Dev 10:672–685. 672 Tolwinski NS, Wieschaus E (2004) Rethinking WNT signaling. Trends Genet 20:177–181. 003 Troyanovsky SM, Troyanovsky RB, Eshkind LG, Krutovskikh VA, Leube RE, Franke WW (1994) Identification of the plakoglobin-binding domain in desmoglein and its role in plaque assembly and intermediate filament anchorage. J Cell Biol 127:151–160 Uemura T, Oda H, Kraut R, Hayashi S, Kotaoka Y, Takeichi M (1996) Zygotic Drosophila Ecadherin expression is required for processes of dynamic epithelial cell rearrangement in the Drosophila embryo.

2 Armadillo Domain of p120 p120 was initially thought to contain as many as 10 arm repeats based on its amino acid sequence (Anastasiadis and Reynolds 2000; Reynolds and Roczniak-Ferguson 2004). A typical arm repeat consists of a ~ 40-residue motif forming three helices (H1, H2 and H3) arranged into a triangular shape (Huber et al. 1997). 2b) (Ishiyama et al. 2010). 2 Å over 324 Cα atoms (Ishiyama et al. 2010). 2b). Though other p120 isoforms contain longer NTR, CTR and insert region than p120-4 A, the structure of the 9-repeat arm domain is likely conserved in all p120 isoforms, as well as other members of the p120-subfamily (p120, ARVCF, δ-catenin and p0071) and the PKP-subfamily (PKP1,-2 and -3) of arm repeat proteins (McCrea and Gu 2010; McCrea and Park 2007).

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