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Cadherin signaling: keeping cells in touch.

Klezovitch O, Vasioukhin V - F1000Res (2015)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Division of Human Biology, Fred Hutchinson Cancer Research Center, Seattle, WA, 98109, USA.

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.

No MeSH data available.


Related in: MedlinePlus

Cadherin-catenin complexes and their role in regulation of major intracellular signaling pathways.The diagram depicts protein members of the adherens junctions clustered at the plasma membranes of two juxtaposed cells and summarizes their individual roles in the intricate network of intracellular signaling pathways. Note that, despite their unique structural features and separate functions, both cadherins and catenins often work in concert and may also participate in the regulation of the same signaling pathway though via a distinct mechanism. Abbreviations: MAPK, mitogen-activated protein kinase; NFκB, nuclear factor-kappa-B; RTK, receptor tyrosine kinase; YAP1, yes-associated protein 1.
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f1: Cadherin-catenin complexes and their role in regulation of major intracellular signaling pathways.The diagram depicts protein members of the adherens junctions clustered at the plasma membranes of two juxtaposed cells and summarizes their individual roles in the intricate network of intracellular signaling pathways. Note that, despite their unique structural features and separate functions, both cadherins and catenins often work in concert and may also participate in the regulation of the same signaling pathway though via a distinct mechanism. Abbreviations: MAPK, mitogen-activated protein kinase; NFκB, nuclear factor-kappa-B; RTK, receptor tyrosine kinase; YAP1, yes-associated protein 1.

Mentions: Cadherin-catenin complexes comprise the core of a specialized type of adhesion junction named an adherens junction (AJ) (Figure 1). Among the family of classic cadherins, which includes E (epithelial)-, N (neural)-, P (placental)-, VE (vascular-endothelial)-, R (retinal)-, and K (kidney)-cadherins, E-cadherin is the most frequently employed in the formation of AJs in epithelial cells. To initiate the adhesion process, extracellular domains of cadherins engage in the Ca2+-dependent homophilic trans-interaction with identical cadherin molecules on an adjacent cell, while their cytoplasmic tails bind to p120- and β- (or its homolog γ-) catenin proteins. In turn, β-catenin interacts with α-catenin, which contains an actin-binding domain and physically links AJ complexes to the actin cytoskeleton1,2. Interaction between the actomyosin cytoskeleton and the AJs is prominently regulated by the mechanical forces and Rho-family of small GTPases (covered in detail in3–6). This regulation is necessary for proper tissue morphogenesis and is highly dynamic, facilitating not only the coupling but also the detachment of cadherin-catenin complexes from actomyosin cytoskeleton, allowing cell-cell separation, cell sorting, and cell migration.


Cadherin signaling: keeping cells in touch.

Klezovitch O, Vasioukhin V - F1000Res (2015)

Cadherin-catenin complexes and their role in regulation of major intracellular signaling pathways.The diagram depicts protein members of the adherens junctions clustered at the plasma membranes of two juxtaposed cells and summarizes their individual roles in the intricate network of intracellular signaling pathways. Note that, despite their unique structural features and separate functions, both cadherins and catenins often work in concert and may also participate in the regulation of the same signaling pathway though via a distinct mechanism. Abbreviations: MAPK, mitogen-activated protein kinase; NFκB, nuclear factor-kappa-B; RTK, receptor tyrosine kinase; YAP1, yes-associated protein 1.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4544379&req=5

f1: Cadherin-catenin complexes and their role in regulation of major intracellular signaling pathways.The diagram depicts protein members of the adherens junctions clustered at the plasma membranes of two juxtaposed cells and summarizes their individual roles in the intricate network of intracellular signaling pathways. Note that, despite their unique structural features and separate functions, both cadherins and catenins often work in concert and may also participate in the regulation of the same signaling pathway though via a distinct mechanism. Abbreviations: MAPK, mitogen-activated protein kinase; NFκB, nuclear factor-kappa-B; RTK, receptor tyrosine kinase; YAP1, yes-associated protein 1.
Mentions: Cadherin-catenin complexes comprise the core of a specialized type of adhesion junction named an adherens junction (AJ) (Figure 1). Among the family of classic cadherins, which includes E (epithelial)-, N (neural)-, P (placental)-, VE (vascular-endothelial)-, R (retinal)-, and K (kidney)-cadherins, E-cadherin is the most frequently employed in the formation of AJs in epithelial cells. To initiate the adhesion process, extracellular domains of cadherins engage in the Ca2+-dependent homophilic trans-interaction with identical cadherin molecules on an adjacent cell, while their cytoplasmic tails bind to p120- and β- (or its homolog γ-) catenin proteins. In turn, β-catenin interacts with α-catenin, which contains an actin-binding domain and physically links AJ complexes to the actin cytoskeleton1,2. Interaction between the actomyosin cytoskeleton and the AJs is prominently regulated by the mechanical forces and Rho-family of small GTPases (covered in detail in3–6). This regulation is necessary for proper tissue morphogenesis and is highly dynamic, facilitating not only the coupling but also the detachment of cadherin-catenin complexes from actomyosin cytoskeleton, allowing cell-cell separation, cell sorting, and cell migration.

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Division of Human Biology, Fred Hutchinson Cancer Research Center, Seattle, WA, 98109, USA.

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.

No MeSH data available.


Related in: MedlinePlus