Adherens junctions and β-catenin-mediated cell signalling in a non-metazoan organism

Grimson, Mark J.; Coates, Juliet C.; Reynolds, Jonathan Peter; Shipman, M.; Blanton, Richard L.; Harwood, Adrian J.

doi:10.1038/35047099

Cited by 131 publications

(113 citation statements)

References 26 publications

Supporting

Mentioning

106

Contrasting

Unclassified

Order By: Relevance

“…Three main components of the Wnt signal transduction cascade, that is, GSK3, CK1, and an ortholog related to b-catenin called Aardvark, have also been found in Dictyostelium (Grimson et al 2000;Coates et al 2002), but other components of the Wnt signal transduction cascade, including Dsh, Axin, and APC proteins, have not been identified (Harwood 2008). A GSK3 ortholog (GSKA) acts in cell growth and differentiation processes of Dictyostelium (Harwood 2008), for example, in the homeostasis of prestalk and prespore cells (Harwood et al 1995;Schilde et al 2004).…”

Section: Wnt Receptors and Mediatorsmentioning

confidence: 99%

See 1 more Smart Citation

The Evolution of the Wnt Pathway

Holstein

2012

Cold Spring Harbor Perspectives in Biology

194

176

View full text Add to dashboard Cite

Wnt genes are important regulators of embryogenesis and cell differentiation in vertebrates and insects. New data revealed by comparative genomics have now shown that members of the Wnt signaling pathway can be found in all clades of metazoans, but not in fungi, plants, or unicellular eukaryotes. This article focuses on new data from recent genomic analyses of several basal metazoan organisms, providing evidence that the Wnt pathway was a primordial signaling pathway during evolution. The formation of a Wnt signaling center at the site of gastrulation was instrumental for the formation of a primary, anterior-posterior body axis, which can be traced throughout animal evolution.

show abstract

Section: Wnt Receptors and Mediatorsmentioning

confidence: 99%

“…The most notable member of the Wnt pathway present in Dictyostelium is the b-cateninrelated molecule Aardvark (Aar) (Grimson et al 2000). Aardvark is essential for the cAMP-mediated induction of pre-spore cells, where it acts together with GSKA.…”

Section: Wnt Receptors and Mediatorsmentioning

confidence: 99%

The Evolution of the Wnt Pathway

Holstein

2012

Cold Spring Harbor Perspectives in Biology

194

176

View full text Add to dashboard Cite

show abstract

“…In the slime mold Dictyostelium discoideum, a betacatenin like gene, Aardvark, seems to fulfill beta-catenin like properties in adhesion and cell specification (Grimson et al, 2000). In yeast, the closest match to metazoan beta-catenin is the vacuolar membrane protein Vac8p (Wang et al, '96;Pan and Goldfarb, '98;Wang et al, '98;Pan et al, 2000) that forms complexes with several proteins.…”

Section: Nonmetazoan Beta-catenins?mentioning

confidence: 99%

Protein evolution: structure‐function relationships of the oncogene beta‐catenin in the evolution of multicellular animals

2003

View full text Add to dashboard Cite

Beta-catenin functions as a cytoskeletal linker protein in cadherin-mediated adhesion and as a signal mediator in wnt-signal transduction pathways. We use a novel integrative approach, combining evolutionary, genomic, and three-dimensional structural data to analyze and trace the structural and functional evolution of beta-catenin genes. This approach also enabled us to examine the effects of gene duplication on the structure and function of beta-catenin genes in Drosophila, C. elegans, and vertebrates. By sampling a large number of different taxa, we identified both ancestral and derived motifs and residues within the different regions of the beta-catenin proteins. Projecting amino acid substitutions onto the three-dimensional structure established for mouse beta-catenin, we identified specific domains that exhibit loss and gain of selective constraints during beta catenin evolution. Structural changes, changes in the amino acid substitution rate, and the appearance of novel functional domains in beta-catenin can be mapped to specific branches on the metazoan tree. Together, our analyses suggest that a single, beta-catenin gene fulfilled both adhesion and signaling functions in the last common ancestor of metazoans some 700 million years ago. In addition, gene duplications facilitated the evolution of beta-catenins with novel functions and allowed the evolution of multiple, single-function proteins (cell adhesion or wnt-signaling) from the ancestral, dual-function protein. Integrative methods such as those we have applied here, utilizing the 'natural experiments' present in animal diversity, can be employed to identify novel and shared functional motifs and residues in virtually any protein among the proteomes of model systems and humans.

show abstract

“…The principle players, the Cadherins, are an ancient family of adhesion molecules, possibly even represented in the social amoeba of Dictyostelium (Wong et al, 1996; see also Grimson et al, 2000), and in the primitive metazoan Hydra (Hobmayer et al, 1996). The extent and diversity of this family has only recently been fully appreciated with the completion of the C. elegans, Drosophila, and human genomes, (Hynes and Zhao, 2000;Nollet et al, 2000;Hill et al, 2001).…”

mentioning

confidence: 99%

Turn‐off, drop‐out: Functional state switching of cadherins

Lilien

Balsamo

Arregui

et al. 2002

Developmental Dynamics

149

116

View full text Add to dashboard Cite

The classic cadherins are a group of calcium dependent, homophilic cell-cell adhesion molecules that drive morphogenetic rearrangements and maintain the integrity of cell groups through the formation of adherens junctions. The formation and maintenance of cadherin-mediated adhesions is a multistep process and mechanisms have evolved to regulate each step. This suggests that functional state switching plays an important role in development. Among the many challenges ahead is to determine the developmental role that functional state switching plays in tissue morphogenesis and to define the roles of each of the several regulatory interactions that participate in switching. One correlate of the loss of cadherinmediated adhesion, the "turn-off" of cadherin function, is the exit, or "drop-out" of cells from neural and epithelial layers and their conversion to a motile phenotype. We suggest that epithelial mesenchymal conversions may be initiated by signaling pathways that result in the loss of cadherin function. Tyrosine phosphorylation of ␤-catenin is one such mechanism. Enhanced phosphorylation of tyrosine residues on ␤-catenin is almost invariably associated with loss of the cadherin-actin connection concomitant with loss of adhesive function. There are several tyrosine kinases and phosphatases that have been shown to have the potential to alter the phosphorylation state of ␤-catenin and thus the function of cadherins. Our laboratory has focused on the role of the nonreceptor tyrosine phosphatase PTP1B in regulating the phosphorylation of ␤-catenin on tyrosine residues. Our data suggest that PTP1B is crucial for maintenance of N-cadherin-mediated adhesions in embryonic neural retina cells. By using an L-cell model system constitutively expressing N-cadherin, we have worked out many of the molecular interactions essential for this regulatory interaction. Extracellular cues that bias this critical regulatory interaction toward increased phosphorylation of ␤-catenin may be a critical component of many developmental events.

show abstract

Adherens junctions and β-catenin-mediated cell signalling in a non-metazoan organism

Cited by 131 publications

References 26 publications

The Evolution of the Wnt Pathway

The Evolution of the Wnt Pathway

Protein evolution: structure‐function relationships of the oncogene beta‐catenin in the evolution of multicellular animals

Turn‐off, drop‐out: Functional state switching of cadherins

Contact Info

Product

Resources

About