Download e-book for iPad: Adherens Junctions: from Molecular Mechanisms to Tissue by Tony J. C. Harris (auth.), Tony Harris (eds.)

By Tony J. C. Harris (auth.), Tony Harris (eds.)

ISBN-10: 9400741855

ISBN-13: 9789400741850

ISBN-10: 9400741863

ISBN-13: 9789400741867

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 bunch of the world over famous specialists studies 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 an essential component of animal evolution, and play critical roles in melanoma improvement, pathogen an infection and different ailments. This publication 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 full phone?
• How do AJs impact cellphone behaviour and multicellular improvement?
• How can irregular AJ task result in disease?

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

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1038/nn1415 Reddy B V, Irvine KD (2008) The Fat and Warts signaling pathways: new insights into their regulation, mechanism and conservation. Development 135:2827–2838. 020974 Reynolds AB, Roesel DJ, Kanner SB, Parsons JT (1989) Transformation-specific tyrosine phosphorylation of a novel cellular protein in chicken cells expressing oncogenic variants of the avian cellular src gene. Mol Cell Biol 9:629–638 Reynolds AB, Daniel J, McCrea PD, Wheelock MJ, Wu J, Zhang Z (1994) Identification of a new catenin: the tyrosine kinase substrate p120cas associates with E-cadherin complexes.

J Cell Biol 171:549–558. 200507072 Dan-Sohkawa MDS, Kaneko HK, Noda KN (1995) Paracellular, transepithelial permeation of macromolecules in the body wall epithelium of starfish embryos. J Exp Zool 271:264–272. 1402710404 Daniel JM, Reynolds AB (1995) The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or α-catenin. Mol Cell Biol 15:4819–4824 Davis MA, Reynolds AB (2006) Blocked acinar development, E-cadherin reduction, and intraepithelial neoplasia upon ablation of p120-catenin in the mouse salivary gland.

The NTR and a large insert within the arm domain of p120 have been shown to interact with Rho-GTPases, such as RhoA and Rac1 (Anastasiadis 2007; Yanagisawa et al. 2008). The recently determined crystal structure of the p120-E-cadherin complex has provided a first look at how this catenin specifically recognizes the cadherin JMD and regulates the internalization of cadherin–catenin complexes via endocytosis (Ishiyama et al. 2010). 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).

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Adherens Junctions: from Molecular Mechanisms to Tissue Development and Disease by Tony J. C. Harris (auth.), Tony Harris (eds.)


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