Abstract
Cadherin-catenin complexes are critical for the assembly of cell-cell adhesion structures known as adherens junctions. In addition to the mechanical linkage of neighboring cells to each other, these cell-cell adhesion protein complexes have recently emerged as important sensors and transmitters of the extracellular cues inside the cell body and into the nucleus. In the past few years, multiple studies have identified a connection between the cadherin-catenin protein complexes and major intracellular signaling pathways. Those studies are the main focus of this review.
Highlights
The ability of cells to communicate and adhere to each other represents an ultimate prerequisite for the formation and maintenance of a multicellular organism
How do the external signals get transmitted inside and prompt the cells to respond ? In the past several years, cadherin-catenin protein complexes emerged as important regulators of morphogenesis and adult tissue homeostasis, linking cell-cell adhesion to multiple major signaling networks
Adherens junctions: structural organization and association with the actin cytoskeleton Cadherin-catenin complexes comprise the core of a specialized type of adhesion junction named an adherens junction (AJ) (Figure 1)
Summary
The ability of cells to communicate and adhere to each other represents an ultimate prerequisite for the formation and maintenance of a multicellular organism. Β- and p120-catenins and the direct line of communication between cell-cell junctions and transcriptional regulation of gene expression By acting at the plasma membrane, cadherins are ideally positioned to attract and retain their cytoplasmic partners, modulating their activation, stability, or nuclear accumulation or a combination of these This is important because some of these intracellular proteins are pivotal signaling molecules in their own right. In Drosophila, the Hippo pathway can be regulated by multiple upstream transmembrane modules, which include atypical cadherins Dachsous and Fat (for review, see 61) Another AJ protein, Echinoid, was shown to activate Hippo signaling via its physical interaction with and stabilization of the Hippo-binding partner Salvador[62]. I confirm that the funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript
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