By Tony J. C. Harris (auth.), Tony Harris (eds.)
Cell–cell adhesion is prime for the advance and homeostasis of animal tissues and organs. Adherens junctions (AJs) are the simplest understood cell-cell adhesion complexes. during this quantity, a gaggle of across the world well-known 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 principal roles in melanoma improvement, pathogen an infection and different illnesses. This booklet 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 full mobile?
• How do AJs have an effect on mobile behaviour and multicellular improvement?
• How can irregular AJ job result in disease?
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Additional info for Adherens Junctions: from Molecular Mechanisms to Tissue Development and Disease
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). 3 p120-E-Cadherin Interfaces Previous deletion and mutagenesis studies have determined that the 18-residue JMDcore region is critical for the binding of E-cadherin with p120, and more importantly for epithelial compaction (Ireton et al.
The arm domain contains nine arm repeats with exon C and a long insert between repeats 5 and 6. The C-terminal region ( CTR) contains exon A and B. Binding sites for various p120-binding partners are indicated. b Crystal structure of the p120 catenin/E-cadherin JMD complex. p120 contains nine arm repeats ( R1–9) with most repeats consisting of three α-helices (H1, H2 and H3), except for R1 and R8 (H3 shown in different colours; PDB codes 3L6X & 3L6Y) (Ishiyama et al. 2010). The JMDcore is shown in magenta (stick and space filling representation).
Indeed, mutations within the cisinterface (V81D/V175D) of E-cadheirn appears to interfere with proper formation of intercellular junctions (Harrison et al. 2011). 6 Post-Translational Modifications Post-translational modifications of classical cadherins are a critical part of modulating the structure and function of cadherin adhesion receptors (Takeichi 1988). First, cadherins are N-glycosylated at numerous sites in the EC domains as part of the quality control process in the endoplasmic reticulum and Golgi network to ensure proper folding and stability (Boggon et al.
Adherens Junctions: from Molecular Mechanisms to Tissue Development and Disease by Tony J. C. Harris (auth.), Tony Harris (eds.)