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 easiest understood cell-cell adhesion complexes. during this quantity, a bunch of across the world famous specialists stories 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 a vital part of animal evolution, and play significant roles in melanoma improvement, pathogen an infection and different illnesses. This ebook addresses significant questions encompassing AJ biology.
• How did AJs evolve?
• How do cadherins and catenins engage to gather AJs and mediate adhesion?
• How do AJs interface with different mobile equipment to couple adhesion with the full cellphone?
• How do AJs have an effect on mobile 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
2010; Thoreson et al. 2000). This interaction is critical for regulating the stability of cadherin–catenin cell–cell adhesion complexes at the cell surface, as downregulation of p120 results in aberrant internalization of cadherins (Davis et al. 2003; Xiao et al. 2003). Consistently, the loss, downregulation or mislocalization of p120 in tumors has been linked to poor prognoses (Thoreson and Reynolds 2002). 2a) (Anastasiadis and Reynolds 2000). Numerous phosphorylation sites have been identified within both NTR and CTR (Mariner et al.
2011; Patel et al. 2006). 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).
The binding of Ca2+ to cadherin is known to make its extracellular region resistant to proteolytic degradation (Takeichi 1988). In contrast, the Ca2+-free state of EC1-5 is more prone to proteolytic cleavage by trypsin, and has been shown to lose its rigidity and adopt a globular shape by EM (Pokutta et al. 1994). The first EC (EC1) domain of cadherin is crucial for the affinity and specificity of its homophilic interaction (Nose et al. 1990; Tomschy et al. 1996). The molecular basis of the underlying dimerization mechanism was first unveiled when the crystal structure of the N-cadherin EC1 domain was determined in a dimeric state (Shapiro et al.
Adherens Junctions: from Molecular Mechanisms to Tissue Development and Disease by Tony J. C. Harris (auth.), Tony Harris (eds.)