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 famous specialists stories 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 significant roles in melanoma improvement, pathogen an infection and different ailments. 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 entire mobile?
• How do AJs impact phone behaviour and multicellular improvement?
• How can irregular AJ task result in disease?

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

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027 Hulpiau P, van Roy F (2010) New Insights into the Evolution of Metazoan Cadherins. Mol Biol Evol 28:647–657. 1093/molbev/msq233 Hyafil F, Babinet C, Jacob F (1981) Cell-cell interactions in early embryogenesis: a molecular approach to the role of calcium. Cell 26:447–454. 1016/0092-8674(81)90214-2 Ireton RC, Davis MA, van Hengel J, Mariner DJ, Barnes K, Thoreson MA, Anastasiadis PZ, Matrisian L, Bundy LM, Sealy L, Gilbert B, van Roy F, Reynolds AB (2002) A novel role for p120 catenin in E-cadherin function.

1a) (Nollet et al. 2000). It can be further divided into two major domains: the juxtramembrane domain (JMD) and the catenin-binding domain (CBD). The JMD consists of ~ 50 residues immediately after the transmembrane domain and provides a specific binding site for p120 catenin and p120-related proteins, such as δ-catenin, ARVCF and p0071 (see below for further discussion) (Ishiyama et al. 2010; Thoreson et al. 2000). On the other hand, the CBD consists of the C-terminal ~ 100 residues and specifically binds to β-catenin and plakoglobin (Huber and Weis 2001) (see below for further discussion).

B The arm repeat 5 of β-catenin contains three α-helices ( H1–3) with a hydrophobic core. c Superposition of the p120/juxtamembrane domain (JMD)core and β-catenin/CBD complexes. p120 ( purple) and β-catenin ( navy) arm domains are shown as cylinders. JMD ( green) and CBD ( cyan) are shown as tubes. d Comparison of the basic arm grooves of p120 and β-catenin. p120 arm repeats 2–4 and β-catenin arm repeats 4–6 (PDB codes 1I7X & 3L6X) are superposed (Ishiyama et al. 2010).

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