alpha Catenin: A catenin that binds F-ACTIN and links the CYTOSKELETON with BETA CATENIN and GAMMA CATENIN.Cytoskeletal Proteins: Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible.Cadherins: Calcium-dependent cell adhesion proteins. They are important in the formation of ADHERENS JUNCTIONS between cells. Cadherins are classified by their distinct immunological and tissue specificities, either by letters (E- for epithelial, N- for neural, and P- for placental cadherins) or by numbers (cadherin-12 or N-cadherin 2 for brain-cadherin). Cadherins promote cell adhesion via a homophilic mechanism as in the construction of tissues and of the whole animal body.Catenins: A family of cytoskeletal proteins that play essential roles in CELL ADHESION at ADHERENS JUNCTIONS by linking CADHERINS to the ACTIN FILAMENTS of the CYTOSKELETON.L Cells (Cell Line): A cultured line of C3H mouse FIBROBLASTS that do not adhere to one another and do not express CADHERINS.beta Catenin: A multi-functional catenin that participates in CELL ADHESION and nuclear signaling. Beta catenin binds CADHERINS and helps link their cytoplasmic tails to the ACTIN in the CYTOSKELETON via ALPHA CATENIN. It also serves as a transcriptional co-activator and downstream component of WNT PROTEIN-mediated SIGNAL TRANSDUCTION PATHWAYS.gamma Catenin: A multi-functional catenin that is highly homologous to BETA CATENIN. Gamma catenin binds CADHERINS and helps link their cytoplasmic tails to ACTIN in the CYTOSKELETON via ALPHA CATENIN. It is also found in DESMOSOMES where it mediates the link between DESMOSOMAL CADHERINS and DESMOPLAKIN.Desmoplakins: Desmoplakins are cytoskeletal linker proteins that anchor INTERMEDIATE FILAMENTS to the PLASMA MEMBRANE at DESMOSOMES.Adherens Junctions: Anchoring points where the CYTOSKELETON of neighboring cells are connected to each other. They are composed of specialized areas of the plasma membrane where bundles of the ACTIN CYTOSKELETON attach to the membrane through the transmembrane linkers, CADHERINS, which in turn attach through their extracellular domains to cadherins in the neighboring cell membranes. In sheets of cells, they form into adhesion belts (zonula adherens) that go all the way around a cell.alpha 1-Antitrypsin: Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.Cell Adhesion Molecules: Surface ligands, usually glycoproteins, that mediate cell-to-cell adhesion. Their functions include the assembly and interconnection of various vertebrate systems, as well as maintenance of tissue integration, wound healing, morphogenic movements, cellular migrations, and metastasis.

The alphaE-catenin gene (CTNNA1) acts as an invasion-suppressor gene in human colon cancer cells. (1/431)

The acquisition of invasiveness is a crucial step in the malignant progression of cancer. In cancers of the colon and of other organs the E-cadherin/catenin complex, which is implicated in homotypic cell-cell adhesion as well as in signal transduction, serves as a powerful inhibitor of invasion. We show here that one allele of the alphaE-catenin (CTNNA1) gene is mutated in the human colon cancer cell family HCT-8, which is identical to HCT-15, DLD-1 and HRT-18. Genetic instability, due to mutations in the HMSH6 (also called GTBP) mismatch repair gene, results in the spontaneous occurrence of invasive variants, all carrying either a mutation or exon skipping in the second alphaE-catenin allele. The alphaE-catenin gene is therefore, an invasion-suppressor gene in accordance with the two-hit model of Knudsen for tumour-suppressor genes.  (+info)

Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin. (2/431)

ZO-2, a member of the MAGUK family, was thought to be specific for tight junctions (TJs) in contrast to ZO-1, another MAGUK family member, which is localized at TJs and adherens junctions (AJs) in epithelial and nonepithelial cells, respectively. Mouse ZO-2 cDNA was isolated, and a specific polyclonal antibody was generated using corresponding synthetic peptides as antigens. Immunofluorescence microscopy with this polyclonal antibody revealed that, similarly to ZO-1, in addition to TJs in epithelial cells, ZO-2 was also concentrated at AJs in nonepithelial cells such as fibroblasts and cardiac muscle cells lacking TJs. When NH2-terminal dlg-like and COOH-terminal non-dlg-like domains of ZO-2 (N-ZO-2 and C-ZO-2, respectively) were separately introduced into cultured cells, N-ZO-2 was colocalized with endogenous ZO-1/ZO-2, i.e. at TJs in epithelial cells and at AJs in non-epithelial cells, whereas C-ZO-2 was distributed along actin filaments. Consistently, occludin as well as alpha catenin directly bound to N-ZO-2 as well as the NH2-terminal dlg-like portion of ZO-1 (N-ZO-1) in vitro. Furthermore, immunoprecipitation experiments revealed that the second PDZ domain of ZO-2 was directly associated with N-ZO-1. These findings indicated that ZO-2 forms a complex with ZO-1/occludin or ZO-1/alpha catenin to establish TJ or AJ domains, respectively.  (+info)

Cadherin-11 is expressed in invasive breast cancer cell lines. (3/431)

In several cancers, including breast cancer, loss of E-cadherin expression is correlated with a loss of the epithelial phenotype and with a gain of invasiveness. Cells that have lost E-cadherin expression are either poorly invasive with a rounded phenotype, or highly invasive, with a mesenchymal phenotype. Most cells lacking E-cadherin still retain weak calcium-dependent adhesion, indicating the presence of another cadherin family member. We have now examined the expression of the mesenchymal cadherin, cadherin-11, in breast cancer cell lines. Cadherin-11 mRNA and protein, as well as a variant form, are expressed in the most invasive cell lines but not in any of the noninvasive cell lines. Cadherin-11 is localized to a detergent-soluble pool and is associated with both alpha- and beta-catenin. Immunocytochemistry shows that cadherin-11 is localized to the cell membrane at sites of cell-cell contact as well as at lamellipodia-like projections, which do not interact with other cells. These results suggest that cadherin-11 expression may be well correlated with the invasive phenotype in cancer cells and may serve as a molecular marker for the more aggressive, invasive subset of tumors. Cadherin-11 may mediate the interaction between malignant tumor cells and other cell types that normally express cadherin-11, such as stromal cells or osteoblasts or perhaps even with the surrounding extracellular matrix, thus facilitating tumor cell invasion and metastasis.  (+info)

Functional domains of alpha-catenin required for the strong state of cadherin-based cell adhesion. (4/431)

The interaction of cadherin-catenin complex with the actin-based cytoskeleton through alpha-catenin is indispensable for cadherin-based cell adhesion activity. We reported previously that E-cadherin-alpha-catenin fusion molecules showed cell adhesion and cytoskeleton binding activities when expressed in nonepithelial L cells. Here, we constructed deletion mutants of E-cadherin-alpha-catenin fusion molecules lacking various domains of alpha-catenin and introduced them into L cells. Detailed analysis identified three distinct functional domains of alpha-catenin: a vinculin/alpha-actinin-binding domain, a ZO-1-binding domain, and an adhesion-modulation domain. Furthermore, cell dissociation assay revealed that the fusion molecules containing the ZO-1-binding domain in addition to the adhesion-modulation domain conferred the strong state of cell adhesion activity on transfectants, although those lacking the ZO-1-binding domain conferred only the weak state. The disorganization of actin-based cytoskeleton by cytochalasin D treatment shifted the cadherin-based cell adhesion from the strong to the weak state. In the epithelial cells, where alpha-catenin was not precisely colocalized with ZO-1, the ZO-1-binding domain did not completely support the strong state of cell adhesion activity. Our studies showed that the interaction of alpha-catenin with the actin-based cytoskeleton through the ZO-1-binding domain is required for the strong state of E-cadherin-based cell adhesion activity.  (+info)

Different behavior of l-afadin and neurabin-II during the formation and destruction of cell-cell adherens junction. (5/431)

We have recently isolated two novel actin filament-binding proteins, l-afadin and neurabin-II and shown that they are localized at cell-cell adherens junction (AJ) in epithelial cells. We found here that l-afadin, neurabin-II, ZO-1, and E-cadherin showed similar and different behavior during the formation and destruction of cell-cell AJ in MDCK cells. In MDCK cells, the accumulation of both l-afadin and E-cadherin, but not that of ZO-1, changed in parallel depending on Rac small G protein activity. Dissociation of MDCK cells by culturing the cells at 2 microM Ca2+ caused rapid endocytosis of E-cadherin, but not that of l-afadin or ZO-1. Addition of phorbol 12-myristate 13-acetate to these dissociated cells formed a tight junction-like structure where ZO-1 and l-afadin, but not neurabin-II or E-cadherin, accumulated. We furthermore found that, in non-epithelial EL cells, which expressed E-cadherin and attached to each other, l-afadin, neurabin-II, ZO-1 and E-cadherin were all localized at AJ. In cadherin-deficient L cells, I-afadin was mainly localized at cell-cell contact sites, but ZO-1 was mainly localized at the tip area of cell processes. Neurabin-II did not accumulate at the plasma membrane area. Neither l-afadin nor neurabin-II significantly interacted with alpha-, beta-catenin, E-cadherin, ZO-1 or occludin.  (+info)

Cell-extracellular matrix interactions and EGF are important regulators of the basal mammary epithelial cell phenotype. (6/431)

The mammary epithelium is composed of a luminal epithelium and a basal layer containing myoepithelial cells and undifferentiated precursors. Basal cells express specific protein markers, such as keratin 14 (K14) and P-cadherin. To study the factors that regulate the basal mammary epithelial cell phenotype, we have established two clonal derivatives of the mouse HC11 cell line, BC20 and BC44, expressing high levels of K14 and P-cadherin. Unlike the parental HC11 cells, these basal cells did not produce beta-casein in response to lactogenic hormone treatment; however their phenotype appeared to be plastic. Cultured in EGF-free medium, they exhibited enhanced cell-extracellular matrix adhesions and deficient cell-cell junctions, whereas long-term treatment with EGF induced a decrease of focal contact number and establishment of cell-cell junctions, resulting in downregulation of K14 and P-cadherin expression at the protein and mRNA levels. To determine whether cell-extracellular matrix interactions mediated by integrins have a role in the regulation of the expression of K14 and P-cadherin, the amounts of transcripts for the two proteins were analysed in the basal cells, which were plated on the function-blocking antibodies against beta1 and alpha6 integrin chains, on fibronectin and on laminin 5. The amount of P-cadherin transcript was 2- to 4-fold higher in cells plated on the function-blocking anti-integrin antibodies and on the extracellular matrix proteins, as compared to cells plated on poly-L-lysine, whereas the K14 transcript levels were not significantly modified in response to adhesion. The data demonstrate that integrin-mediated cell interaction with extracellular matrix is directly implicated in the control of P-cadherin expression, and that EGF and cell-extracellular matrix adhesion events are important regulators of the basal mammary epithelial cell phenotype.  (+info)

Rearrangement of adherens junctions by transforming growth factor-beta1: role of contraction. (7/431)

The signal transduction pathways that lead to disruption of pulmonary endothelial monolayer integrity by transforming growth factor-beta1 (TGF-beta1) have not been elucidated. The purpose of this investigation was to determine whether disassembly of the adherens junction is temporally associated with the TGF-beta1-induced decrease in pulmonary endothelial monolayer integrity. Measurement of albumin clearance and electrical resistance showed that monolayer integrity started to decrease between 1 and 2 h post-TGF-beta1 treatment and continued to slowly decrease over the next 6 h. Immunofluorescence microscopy of monolayers between 2 and 3 h post-TGF-beta1 showed that beta-catenin, plakoglobin, alpha-catenin, and cadherin-5 were colocalized both at the cell periphery and in newly formed bands that are perpendicular to the cell-cell border. At 4 h post-TGF-beta1, cells began separating; however, beta- and alpha-catenin, plakoglobin, and cadherin-5 could still be found at the cell periphery at areas of cell separation and in strands between separated cells. By 8 h, these junctional proteins were no longer present at the cell periphery at areas of cell separation. The myosin light chain kinase inhibitor KT-5926 prevented the TGF-beta1-induced change in integrity but did not inhibit the formation of actin stress fibers or the formation of bands containing adherens junction proteins that were perpendicular to the cell-cell junction. Overall, these results suggest that adherens junction disassembly occurs after cell separation during TGF-beta1-induced decreases in pulmonary endothelial monolayer integrity and that the loss of integrity may be due to the activation of a myosin light chain kinase-dependent signaling cascade.  (+info)

E-cadherin and alpha-, beta- and gamma-catenin expression in prostate cancers: correlation with tumour invasion. (8/431)

The E-cadherin-catenin complex plays an important role in establishing and maintaining intercellular connections and morphogenesis and reduced expression of its constituent molecules is associated with invasion and metastasis. In the present study, we examined E-cadherin and alpha-, beta- and gamma-catenin levels in tumour tissues obtained by radical prostatectomy in order to investigate the relationship with histopathological tumour invasion. Immunohistochemical findings for 45 prostate cancer specimens demonstrated aberrant expression of each molecule to be associated with dedifferentiation and, in addition, alteration of staining patterns for the three types of catenin was significantly correlated with capsular but not lymphatic or vascular invasion. The data thus suggest that three types of catenin may be useful predictive markers for biological aggressiveness of prostate cancer.  (+info)

*Catenin

Zhang F, Meng F, Li H, Dong Y, Yang W, Han A (September 2011). "Suppression of retinoid X receptor alpha and aberrant β-catenin ... α-catenin β-catenin δ-catenin γ-catenin All but α-catenin contain armadillo repeats. Several types of catenins work with N- ... The first two catenins that were identified became known as α-catenin and β-catenin. A-catenin can bind to β-catenin and can ... B-catenin binds the cytoplasmic domain of some cadherins. Additional catenins such as γ-catenin and δ-catenin have been ...

*Cell adhesion molecule

Integrins are heterodimeric, as they consist of an alpha and beta subunit. There are currently 18 alpha subunits and 8 beta ... The cytoplasmic domain has specific regions where catenin proteins bind. The selectins are a family of heterophilic CAMs that ... Within each of the alpha and beta subunits there is a large extracellular domain, a transmembrane domain and a short ... which link to the actin filament network through specific linking proteins called catenins. Each cadherin exhibits a unique ...

*Alpha catenin

... alpha-2-catenin (also called alpha-N-catenin) alpha-3-catenin (also called alpha-T-catenin) Catenin alpha Catenin at the US ... There are three human alpha-catenin genes: alpha-1-catenin (also called alpha-E-catenin) ... beta-catenin and alpha-catenin has not been isolated. It has been suggested that alpha-catenin does not bind with high affinity ... "Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin". J. Cell Biol. 130 (1): 67 ...

*Catenin alpha-1

αE-catenin, also known as Catenin alpha-1 is a protein that in humans is encoded by the CTNNA1 gene. αE-catenin is highly ... αE-catenin has been shown to interact with: APC, Beta-catenin, CDH1, CDH2, CDH3 Plakoglobin, and VE-cadherin. Alpha catenin ... Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin ... "Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin". J. Cell Biol. 130 (1): 67 ...

*Vinculin family

Three different types of catenins seem to exist: alpha, beta, and gamma. Alpha-catenins are proteins of about 100 kDa which are ... in alpha-catenin, of the repeated domain and of the proline-rich segment. Vinculin InterPro: IPR000633 Alpha-catenin InterPro: ... Alpha-catenins are evolutionary related to vinculin. Catenins are proteins that associate with the cytoplasmic domain of a ... Lottspeich F, Eckerskorn C, Herrenknecht K, Ozawa M, Lenter M, Kemler R (1991). "The uvomorulin-anchorage protein alpha catenin ...

*CDH3 (gene)

... has been shown to interact with: Beta-catenin, CDH1, Catenin (cadherin-associated protein), alpha 1, Nephrin and ... "The uvomorulin-anchorage protein alpha catenin is a vinculin homologue". Proceedings of the National Academy of Sciences of the ... Reynolds AB, Daniel JM, Mo YY, Wu J, Zhang Z (Jun 1996). "The novel catenin p120cas binds classical cadherins and induces an ...

*CDH2

"Identification of plakoglobin domains required for association with N-cadherin and alpha-catenin". J. Biol. Chem. 270 (34): ... N-cadherins interact with catenins to play an important role in learning and memory (For full article see Cadherin-catenin ... Wahl JK, Kim YJ, Cullen JM, Johnson KR, Wheelock MJ (May 2003). "N-cadherin-catenin complexes form prior to cleavage of the ... Lu Q, Paredes M, Medina M, Zhou J, Cavallo R, Peifer M, Orecchio L, Kosik KS (1999). "delta-catenin, an adhesive junction- ...

*CTNNAL1

Janssens B, Staes K, van Roy F (1999). "Human alpha-catulin, a novel alpha-catenin-like molecule with conserved genomic ... Merdek KD, Nguyen NT, Toksoz D (2004). "Distinct Activities of the α-Catenin Family, α-Catulin and α-Catenin, on β-Catenin- ... "Association of Lbc Rho guanine nucleotide exchange factor with alpha-catenin-related protein, alpha-catulin/CTNNAL1, supports ... "Association of Lbc Rho guanine nucleotide exchange factor with alpha-catenin-related protein, alpha-catulin/CTNNAL1, supports ...

*ALCAM

2000). "Coordinate recruitment of E-cadherin and ALCAM to cell-cell contacts by alpha-catenin". Biochem. Biophys. Res. Commun. ...

*Epithelial polarity

"Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin". J. Cell Biol. 130 (1): 67 ... cellular domains of E-cadherin molecules bind to the actin cytoskeleton via the adaptor proteins alpha-catenin and beta-catenin ...

*JUB (gene)

"The LIM protein Ajuba is recruited to cadherin-dependent cell junctions through an association with alpha-catenin". J. Biol. ...

*Plakoglobin

"Identification of the domain of alpha-catenin involved in its association with beta-catenin and plakoglobin (gamma-catenin)". ... "A mutation in alpha-catenin disrupts adhesion in clone A cells without perturbing its actin and beta-catenin binding activity ... "The APC protein and E-cadherin form similar but independent complexes with alpha-catenin, beta-catenin, and plakoglobin". The ... "The APC protein and E-cadherin form similar but independent complexes with alpha-catenin, beta-catenin, and plakoglobin". The ...

*CDH1 (gene)

Beta-catenin can also bind to alpha-catenin. Alpha-catenin participates in regulation of actin-containing cytoskeletal ... Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin ... "A truncated beta-catenin disrupts the interaction between E-cadherin and alpha-catenin: a cause of loss of intercellular ... Loss of E-cadherin expression results in releasing β-catenin into the cytoplasm. Liberated β-catenin molecules may migrate into ...

*Tight junction protein 1

"Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filaments". The ... "Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filaments". The ... a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin ... a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin ...

*FYN

Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin ... Kihara T, Shimohama S, Sawada H, Honda K, Nakamizo T, Shibasaki H, Kume T, Akaike A (April 2001). "alpha 7 nicotinic receptor ... Martinez MC, Ochiishi T, Majewski M, Kosik KS (July 2003). "Dual regulation of neuronal morphogenesis by a delta-catenin- ...

*YES1

Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin ...

*ARHGEF1

"Association of Lbc Rho guanine nucleotide exchange factor with alpha-catenin-related protein, alpha-catulin/CTNNAL1, supports ... "RGS16 inhibits signalling through the G alpha 13-Rho axis". Nat. Cell Biol. 5 (12): 1095-103. doi:10.1038/ncb1065. PMID ... Bhattacharyya R, Wedegaertner PB (2003). "Characterization of G alpha 13-dependent plasma membrane recruitment of p115RhoGEF". ...

*CTNND1

Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin ... alpha 1, Cortactin, FYN, MUC1, Nephrin, PSEN1, PTPN6, PTPRJ, PTPRM, VE-cadherin, YES1, and ZBTB33 Delta catenin Catenin CTNND2 ... Catenin delta-1 is a protein that in humans is encoded by the CTNND1 gene. This gene encodes a member of the Armadillo protein ... "Entrez Gene: CTNND1 catenin (cadherin-associated protein), delta 1". Hazan RB, Norton L (April 1998). "The epidermal growth ...

*AKAP13

"Association of Lbc Rho guanine nucleotide exchange factor with alpha-catenin-related protein, alpha-catulin/CTNNAL1, supports ... "Association of Lbc Rho guanine nucleotide exchange factor with alpha-catenin-related protein, alpha-catulin/CTNNAL1, supports ... AKAP13 has been shown to interact with Estrogen receptor alpha, CTNNAL1 and PRKAR2A. GRCh38: Ensembl release 89: ...

*Actinin alpha 1

"Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin". J. Cell Biol. 130 (1): 67 ... Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 gene. Alpha actinins belong to the spectrin gene ... Actinin, alpha 1 has been shown to interact with: CDK5R1, CDK5R2, Collagen, type XVII, alpha 1, GIPC1, PDLIM1, Protein kinase ... 1999). "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". ...

*TCF7L2

... nuclear import of alpha-catenin by the beta-catenin/Tcf complex". Experimental Cell Research. 255 (2): 207-20. doi:10.1006/excr ... It is a member of the TCF family that can form a bipartite transcription factor (β-catenin/TCF) alongside β-catenin. Bipartite ... TCF7L2 is downstream of the WNT/β-catenin pathways. The activation of the WNT/β-catenin pathways have been associated ... Tang W, Dodge M, Gundapaneni D, Michnoff C, Roth M, Lum L (July 2008). "A genome-wide RNAi screen for Wnt/beta-catenin pathway ...

*Occludin

... a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin ... a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin ... "Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-beta-catenin complexes from the cytoskeleton by ...

*Tight junction protein 2

... a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin ... a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin ...

*Adenomatous polyposis coli

... kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin". ... The researchers hypothesized that APC's many β-catenin binding site increase the protein's efficiency at destroying β-catenin, ... interacts with beta-catenin, GSK-3beta and APC and reduces the beta-catenin level". Genes to Cells. 3 (6): 395-403. doi:10.1046 ... GSK-3β is able to phosphorylate β-catenin a second time. This targets β-catenin for ubiquitination and degradation by cellular ...

*Beta-catenin

Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin ... This is possible because α-catenin and cadherins bind at distinct sites to β-catenin. The β-catenin - α-catenin complex can ... Specifically, beta-catenin is part of a distinct complex with N-cadherin and alpha-catenin, which is abundant at adherens ... Although the precise details are much less clear, it appears that the same site is used by alpha-catenin when beta-catenin is ...

*Androgen

Also, androgens, but not estrogens, increase beta adrenergic receptors while decreasing alpha adrenergic receptors- which ... nuclear translocation of androgen receptor complex with beta-catenin and T-cell factor 4 may bypass canonical Wnt signaling to ... results in increased levels of epinephrine/ norepinephrine due to lack of alpha-2 receptor negative feedback and decreased fat ...

*Focal adhesion targeting region

... alpha-catenin and vinculin. The binding of FAT to the focal adhesion protein, paxillin, requires the integrity of the helical ...
Catenin Beta 1, CTNNB are cell adhesion molecules called (p120*␠-catenin) cadherins (the (CDH1) E-cadherin/catenin complex) include the beta-catenins a multifunctional molecule Locus: 3p22.1 [§§; ^]. Neurons also exhibited a higher CTNNB/TCF pathway association (concentration versus accumulation) with cadherins; CAS-chromosome segregation 1-like (yeast) binds with E-cadherin but not with beta-catenin. Which interacts with (Tcf-T-cell factor where a…
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Complete information for CTNNA1 gene (Protein Coding), Catenin Alpha 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Human CTNNA2 qPCR primer pairs, confirmed in positive organizations; screened the primer with high specificity and high sensitivity.
The cadherin-catenin complex is important for mediating homotypic, calcium-dependent cell-cell interactions in diverse tissue types. Although proteins of this complex have been identified, little is known about their interactions. Using a genetic assay in yeast and an in vitro protein-binding assay, we demonstrate that beta-catenin is the linker protein between E-cadherin and alpha-catenin and that E-cadherin does not bind directly to alpha-catenin. We show that a 25-amino acid sequence in the cytoplasmic domain of E-cadherin and the amino-terminal domain of alpha-catenin are independent binding sites for beta-catenin. In addition to beta-catenin and plakoglobin, another member of the armadillo family, p120 binds to E-cadherin. However, unlike beta-catenin, p120 does not bind alpha-catenin in vitro, although a complex of p120 and endogenous alpha-catenin could be immunoprecipitated from cell extracts. In vitro protein-binding assays using recombinant E-cadherin cytoplasmic domain and ...
In vitro studies with purified proteins showed that αE-catenin is an allosteric protein in which the monomer binds the cadherin-catenin complex and homodimer preferentially binds actin filaments and inhibits Arp2/3 complex-mediated actin polymerization (Drees et al., 2005; Yamada et al., 2005). These results intimated roles for αE-catenin in the regulation of actin-based membrane dynamics in addition to and perhaps independent of αE-catenin roles in cell-cell adhesion. In this study, we tested key predictions of these in vitro results in epithelial cells.. We identified multiple forms of αE-catenin in MDCK cells. A membrane-bound pool of αE-catenin was identified in the E-cadherin-catenin complex; formally, we do not know whether this pool is a monomer, homodimer, or both, although it is likely to be a monomer based upon structural evidence (Pokutta and Weis, 2000). In the cytosol, we identified αE-catenin monomer and homodimer, which had a relatively fast turnover rate. We also observed ...
In vitro studies with purified proteins showed that αE-catenin is an allosteric protein in which the monomer binds the cadherin-catenin complex and homodimer preferentially binds actin filaments and inhibits Arp2/3 complex-mediated actin polymerization (Drees et al., 2005; Yamada et al., 2005). These results intimated roles for αE-catenin in the regulation of actin-based membrane dynamics in addition to and perhaps independent of αE-catenin roles in cell-cell adhesion. In this study, we tested key predictions of these in vitro results in epithelial cells.. We identified multiple forms of αE-catenin in MDCK cells. A membrane-bound pool of αE-catenin was identified in the E-cadherin-catenin complex; formally, we do not know whether this pool is a monomer, homodimer, or both, although it is likely to be a monomer based upon structural evidence (Pokutta and Weis, 2000). In the cytosol, we identified αE-catenin monomer and homodimer, which had a relatively fast turnover rate. We also observed ...
A key component of the Wnt pathway, beta-catenin combines with alpha-catenin and regulates cell-cell adhesion. It also interacts with alpha-catenin in the nucleus.. The alpha-catenin component of this beta-catenin/alpha-catenin complex has an inhibitory effect on beta-catenin that helps keep tumor cell migration and invasion in check. This inhibition is lost, however, when the EGFR pathway is activated. Upon activation, beta-catenin becomes untethered from alpha-catenin and translocates to the cell nucleus, where it increases expression of key target genes involved in tumor cell invasion and metastasis.. New Pathway Regulates Beta-Catenin Transactivation. The M. D. Anderson-led team made a surprising discovery: Beta-catenin also can travel to the nucleus via activation of the EGFR pathway-and it does so independently of Wnt signaling or mutations. The newly described pathway disrupts the beta-catenin/alpha catenin complex through an EGFR-extracellular receptor kinase (ERK)-protein kinase CK2- ...
The increased penetrance, earlier onset, and increased severity of the cardiac phenotype in αMHC/Ecad mice suggests that the epithelial cadherin may further perturb the transmission of the contractile force across the intercalated disc structure. In contrast to chick N-cadherin, the less similar E-cadherin is more likely to interfere with adherens junction organization by intercalating into the cadherin zipper, thus disrupting the normal homogeneous clustering of N-cadherin/catenin complexes ( Fig. 9). Mouse and chicken N-cadherin are nearly identical in the cytoplasmic and transmembrane domains; therefore, we predict normal interaction(s) with the submembranous myofibril connection. In comparison, the cytoplasmic domain of E-cadherin is less similar (61%) and somewhat shorter (10 amino acids) than N-cadherin. Although TEM did not indicate any obvious defect in myofibril insertion at the cell membrane, it is possible that subtle molecular differences in the E-cadherin/myofibril connection may ...
Polyclonal antibody for ALPHA 1 CATENIN/CTNNA1 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. ALPHA 1 CATENIN/CTNNA1 information: Molecular Weight: 100071 MW; Subcellular Localization: Isoform 1: Cytoplasm,
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TY - JOUR. T1 - The cadherin-catenin adhesion system in signaling and cancer. AU - Conacci-Sorrell, Maralice. AU - Zhurinsky, Jacob. AU - Ben-Zeev, Avri. PY - 2002/4/29. Y1 - 2002/4/29. UR - http://www.scopus.com/inward/record.url?scp=0036120562&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0036120562&partnerID=8YFLogxK. U2 - 10.1172/JCI200215429. DO - 10.1172/JCI200215429. M3 - Review article. C2 - 11956233. AN - SCOPUS:0036120562. VL - 109. SP - 987. EP - 991. JO - Journal of Clinical Investigation. JF - Journal of Clinical Investigation. SN - 0021-9738. IS - 8. ER - ...
Synapses are fundamental building blocks of neural circuits. Synapse formation requires complex regulation involving cell adhesion molecules, secreted molecules, transcription factors and so forth. For cell adhesion molecules, ...
β-Catenin is essential for muscle development because it regulates both cadherin-mediated cell-cell adhesion and canonical Wingless and Int1 (Wnt) signaling. The phosphorylation of β-catenin by glycogen synthase kinase-3β (GSK-3β) at serine31/37/
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The gene encoding α-T-catenin, CTNNA3,is positioned within a region on chromosome 10, showing strong evidence of linkage to Alzheimers disease (AD), and is therefore a good positional candidate...
The cadherin-catenin complex (CCC) is crucial for successful completion of morphogenesis during embryonic development, and for suppression of metastatic phenoty...
Expression of CTNNA2 (CAP-R, CT114) in cancer tissue. The cancer tissue page shows antibody staining of the protein in 20 different cancers.
Background: Approximately one third of the hereditary diffuse gastric cancer (HDGC) families carry germline mutations in the E-cadherin gene (CDH1). Risk prediction in members of families with this rare but deadly cancer could be improved by the identification of additional HDGC genes in non-CDH1 families.. Methods: Affected individuals from 22 CDH1 mutation-negative families were screened for germline mutations in four catenin genes: CTNNA1, CTNNB1, JUP, and CTNND1. Catenins interact closely with E-cadherin molecules in cells, and are therefore logical candidate genes for mutation screening in HDGC families.. Results: No nonsynonymous variants were seen in CTNNA1, CTNNB1, or CTNND1; only JUP contained nonsynonymous variants, of which only two rare variants were predicted to be deleterious.. Conclusion: Catenin genes are not commonly mutated in non-CDH1 HDGC families.. Impact: Germline mutations in CTNNA1, CTNNB1, JUP, or CTNND1 are unlikely to play a major role in HDGC. Cancer Epidemiol ...
BACKGROUND: Approximately one third of the hereditary diffuse gastric cancer (HDGC) families carry germline mutations in the E-cadherin gene (CDH1). Risk prediction in members of families with this rare but deadly cancer could be improved by the identification of additional HDGC genes in non-CDH1 families.METHODS: Affected individuals from 22 CDH1 mutation-negative families were screened for germline mutations in four catenin genes: CTNNA1, CTNNB1, JUP, and CTNND1. Catenins interact closely with E-cadherin molecules in cells, and are therefore logical candidate genes for mutation screening in HDGC families.RESULTS: No nonsynonymous variants were seen in CTNNA1, CTNNB1, or CTNND1; only JUP contained nonsynonymous variants, of which only two rare variants were predicted to be deleterious.CONCLUSION: Catenin genes are not commonly mutated in non-CDH1 HDGC families.Impact: Germline mutations in CTNNA1, CTNNB1, JUP, or CTNND1 are unlikely to play a major role in HDGC. Cancer Epidemiol Biomarkers Prev; 1-3.
Cell-cell adherens junctions (AJs), the most common type of intercellular adhesions, are important for maintaining tissue architecture and cell polarity and can limit cell movement and proliferation. At AJs, E-cadherin serves as an essential cell adhesion molecules (CAMs). The cytoplasmic tail binds beta-catenin, which in turn binds alpha-catenin. Alpha-catenin is associated with F-actin bundles directly and indirectly. The integrity of the cadherin-catenin complex is negatively regulated by phosphorylation of beta-catenin by receptor tyrosine kinases (RTKs) and cytoplasmic tyrosine kinases (Fer, Fyn, Yes, and Src), which leads to dissociation of the cadherin-catenin complex. Integrity of this complex is positively regulated by beta -catenin phosphorylation by casein kinase II, and dephosphorylation by protein tyrosine phosphatases. Changes in the phosphorylation state of beta-catenin affect cell-cell adhesion, cell migration and the level of signaling beta-catenin. Wnt signaling acts as a ...
Cell-cell adherens junctions (AJs), the most common type of intercellular adhesions, are important for maintaining tissue architecture and cell polarity and can limit cell movement and proliferation. At AJs, E-cadherin serves as an essential cell adhesion molecules (CAMs). The cytoplasmic tail binds beta-catenin, which in turn binds alpha-catenin. Alpha-catenin is associated with F-actin bundles directly and indirectly. The integrity of the cadherin-catenin complex is negatively regulated by phosphorylation of beta-catenin by receptor tyrosine kinases (RTKs) and cytoplasmic tyrosine kinases (Fer, Fyn, Yes, and Src), which leads to dissociation of the cadherin-catenin complex. Integrity of this complex is positively regulated by beta -catenin phosphorylation by casein kinase II, and dephosphorylation by protein tyrosine phosphatases. Changes in the phosphorylation state of beta-catenin affect cell-cell adhesion, cell migration and the level of signaling beta-catenin. Wnt signaling acts as a ...
Cell-cell adherens junctions (AJs), the most common type of intercellular adhesions, are important for maintaining tissue architecture and cell polarity and can limit cell movement and proliferation. At AJs, E-cadherin serves as an essential cell adhesion molecules (CAMs). The cytoplasmic tail binds beta-catenin, which in turn binds alpha-catenin. Alpha-catenin is associated with F-actin bundles directly and indirectly. The integrity of the cadherin-catenin complex is negatively regulated by phosphorylation of beta-catenin by receptor tyrosine kinases (RTKs) and cytoplasmic tyrosine kinases (Fer, Fyn, Yes, and Src), which leads to dissociation of the cadherin-catenin complex. Integrity of this complex is positively regulated by beta -catenin phosphorylation by casein kinase II, and dephosphorylation by protein tyrosine phosphatases. Changes in the phosphorylation state of beta-catenin affect cell-cell adhesion, cell migration and the level of signaling beta-catenin. Wnt signaling acts as a ...
Cadherins are calcium-dependent, cell surface glycoproteins involved in cell-cell adhesion. To function in cell-cell adhesion, the transmembrane cadherin molecule must be associated with the cytoskeleton via cytoplasmic proteins known as catenins. Three catenins, alpha-catenin, beta-catenin, and gamma-catenin (also known as plakoglobin), have been identified. The domain of the cadherin molecule important for its interaction with the catenins has been mapped to the COOH-terminal 70 amino acids, but less is known about regions of the catenins that allow them to associate with one another or with the cadherin molecule. In this study we have transfected carboxyl-terminal deletions of plakoglobin into the human fibrosarcoma HT-1080 and used immunofluorescence localization and co-immunoprecipitation to map the regions of plakoglobin that allow it to associate with N-cadherin and with alpha-catenin. Plakoglobin is an armadillo family member containing 13 weakly similar internal repeats. These data show ...
Cadherins are calcium-dependent, cell surface glycoproteins involved in cell-cell adhesion. To function in cell-cell adhesion, the transmembrane cadherin molecule must be associated with the cytoskeleton via cytoplasmic proteins known as catenins. Three catenins, alpha-catenin, beta-catenin, and gamma-catenin (also known as plakoglobin), have been identified. The domain of the cadherin molecule important for its interaction with the catenins has been mapped to the COOH-terminal 70 amino acids, but less is known about regions of the catenins that allow them to associate with one another or with the cadherin molecule. In this study we have transfected carboxyl-terminal deletions of plakoglobin into the human fibrosarcoma HT-1080 and used immunofluorescence localization and co-immunoprecipitation to map the regions of plakoglobin that allow it to associate with N-cadherin and with alpha-catenin. Plakoglobin is an armadillo family member containing 13 weakly similar internal repeats. These data show ...
We show in this paper that this can indeed occur, in a cell culture system in which Wg signaling can be controlled and its response be measured over time. We found two contrasting effects: Wg initially lowers the amount of the cadherin-catenin complex at cell-cell contacts, most probably by reducing the Arm pool interacting with E-cadherin, but later, Wg signaling leads to elevated DE-cadherin transcription. This later increase in DE cadherin may titrate the pool of Arm available for Wg signaling and therefore attenuate the transcriptional response to Wg. We have shown by metabolic labeling experiments that the reduction in E-cadherin levels was caused by a posttranscriptional mechanism that affected the stability of the E-cadherin protein. Although levels of E-cadherin precursors were similar in the absence or presence of Wg signaling, very little mature E-cadherin was detectable in cells with an activated Wg pathway, indicating that the majority of E-cadherin was either degraded before arrival ...
BACKGROUND: In approximately 10% of all gastric cancer (GC) cases, a heritable cause is suspected. A subset of these cases have a causative germline CDH1 mutation; however, in most cases the cause remains unknown. Our objective was to assess to what extent these remaining cases may be explained by germline mutations in the novel candidate GC predisposing genes CTNNA1, MAP3K6 or MYD88. METHODS: We sequenced a large cohort of unexplained young and/or familial patients with GC (n=286) without a CDH1germline mutation for germline variants affecting CTNNA1, MAP3K6 and MYD88 using a targeted next-generation sequencing approach based on single-molecule molecular inversion probes ...
CTNNB1 - CTNNB1 (GFP-tagged) - Human catenin (cadherin-associated protein), beta 1, 88kDa (CTNNB1), transcript variant 2 available for purchase from OriGene - Your Gene Company.
When we examined solid pseudopapillary tumours of the pancreas, a tumour characterised by β‐catenin mutations within exon 3, these tumours showed a strong reduction in E‐cadherin:β‐catenin complexes. Moreover in HCC, a tumour type which has approximately 20% β‐catenin exon 3 mutations, there was a good correlation between reduction in E‐cadherin and activation of Wnt signalling targets. Thus, it may be that in these cancers, E‐cadherin limits the precise levels of Wnt signalling driven by β‐catenin mutation. Thus, downregulation of E‐cadherin in these tumours may drive tumour progression. It should also be noted that opposing patterns of Wnt signalling and E‐cadherin have been shown in murine liver, with β‐catenin higher in zone 3 of the liver and E‐cadherin in zone 1. Therefore, one might predict that β‐catenin mutations would yield a greater phenotype in hepatocytes from zone 3 of the liver versus zone 1 (Benhamouche et al, 2006). Hence, one could speculate ...
My work examines the role of a conserved tryptophan residue, Trp2, in the adhesive domain of cadherins that has been shown to be essential for their adhesive function. Structural studies have shown Trp2 to be integrated into its own cadherin domain, integrated into the domain an opposing cadherin molecule, or freed from the domain and exposed to solvent. Until now, the physiological relevance of these structures has been controversial. Using conformation specific antibodies I show that Trp2 integrates into the domain fold of its own cadherin molecule in physiological conditions, but that this integration is not stable owing to structural constraints imposed by calcium binding to the cadherin. This raises the possibility that Trp2 could participate in intermolecular interactions during adhesion by inserting into opposing cadherins in what is referred to as the strand exchange model of cadherin adhesion. This model is tested directly by introducing cysteine substitutions into opposing cadherins ...
Regulating the cytosolic concentration of the protein β-catenin is an important cell proliferation control mechanism. The cytoplasmic concentration of β-catenin remains low through an interaction with a protein complex consisting of adenomatous polyposis coli (APC), Axin, protein phosphatase 2A, and glycogen synthase kinase 3β (GSK3β). Upon phosphorylation by GSK3β, β-catenin associates with a ubiquitin ligase (E3) complex, resulting in its ubiquitination and proteolysis. Activation of Wnt signaling inactivates GSK3, allowing β-catenin to accumulate in the cytoplasm and eventually to translocate to the nucleus so as to affect gene expression. Two groups report that a phosphorylation-independent mechanism can lead to the destruction of β-catenin. Matsuzawa and Reed show that a mammalian protein called Siah-1 lies at the hub of another pathway that destroys β-catenin in response to DNA damaging agents and the activation of the tumor suppressor protein p53. Siah-1 is known to interact with ...
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Our study unveils a TREM2/β-catenin pathway that regulates bone mass by regulating the rate of OC generation. Mechanistically, TREM2 and β-catenin augment the M-CSF-induced proliferation of OcP, retarding their differentiation into mature OC. Ablation of either TREM2 or β-catenin inhibits the proliferation of OcP, accelerating their differentiation into bone-resorbing OC, which ultimately cause osteoporosis. The possibility that TREM2 and β-catenin act along the same pathway is supported not only by the similar osteoporotic phenotypes of TREM2−/− and βcatΔ/Δ mice, but also by genetic evidence that simultaneous heterozygosity for TREM2- and β-catenin-null alleles results in osteoporosis, whereas no phenotype is observed in mice heterozygous for either of these alleles.. TREM2 may enhance M-CSF-induced activation of β-catenin by facilitating the recruitment of DAP12 to the receptor for M-CSF. In turn, DAP12 may activate Syk and Pyk2, which promote phosphorylation and nuclear ...
Levels of β-catenin and phospho-β-catenin (p-β-catenin), and their subcellular localization.In HB1.F3, β-catenin is mainly localized in nucleus (A), and p-
The present invention relates to mounting and adhesion systems and methods for compact electronic modules. More particularly, the present invention relates to an apparatus and technique for mounting an electronic module that is capable of communicating with an interface unit on a one-way-bus.
gamma-catenin Antibody (F-2) is a monoclonal anti-γ-catenin antibody that detects m, r, and h γ-catenin by WB, IP, IF and ELISA.
δ-catenin interacts directly with the juxtamembrane region of cadherins in the yeast two-hybrid system. (A) Interaction of δ-catenin with various cadherin fr
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β-Catenin is essential for embryonic development and required for cell renewal/regeneration in adult life. Cellular β-catenin exists in three different pools: membranous, cytoplasmic and nuclear. In...
Antibody Sampler Kit for studying Catenin-alphaE/Catenin-beta/E-Cadherin/N-Cadherin/P-Cadherin/R-cadherin in the Adhesion research area.
Mutations in the Wnt/-catenin pathway occur in most colorectal cancers (CRCs), and these mutations lead to increased nuclear accumulation of the -catenin transcriptional co-activator. element within the first intron of the gene to drive expression in CRC cells. As such, reducing -catenin expression in CRC cells using shRNAs leads to decreased mRNA and protein levels. …Read More. ...
The canonical WNT-β-catenin pathway is essential for self-renewal, growth and survival of AML stem/blast progenitor cells (BPCs). Deregulated WNT signaling inhibits degradation of β-catenin, causing increased nuclear translocation and co-factor activity of β-catenin with the transcriptional regulator TCF4/LEF1 in AML BPCs. Here, we determined the pre-clinical anti-AML activity of the ...
TY - JOUR. T1 - Ras farnesylation inhibitor FTI-277 restores the E-cadherin/catenin cell adhesion system in human cancer cells and reduces cancer metastasis. AU - Nam, Jeong Seok. AU - Ino, Yoshinori. AU - Sakamoto, Michiie. AU - Hirohashi, Setsuo. PY - 2002/9/1. Y1 - 2002/9/1. N2 - The E-cadherin/catenin cell adhesion system is often down-regulated in epithelial tumors. This is thought to play an important role in cancer invasion and metastasis, and restoration of this system may suppress metastatic spread of cancer. In this study, the effects of a Ras farnesylation inhibitor (FTI-277) on E-cadherin-mediated cell-cell adhesion and metastatic potential were examined. In cell aggregation assays, FTI-277 stimulated aggregation of colon, liver and breast cancer cells. In vitro cultures of cancer cells showed that FTI-277 induced strong cell-cell contact. Immunoblotting analysis showed that FTI-277 increased E-cadherin/catenin (α, β and γ) expression and strongly stabilized E-cadherin/catenin ...
Catenins are a family of proteins found in complexes with cadherin cell adhesion molecules of animal cells. The first two catenins that were identified became known as α-catenin and β-catenin. A-catenin can bind to β-catenin and can also bind actin. B-catenin binds the cytoplasmic domain of some cadherins. Additional catenins such as γ-catenin and δ-catenin have been identified. The name "catenin" was originally selected (catena means chain in Latin) because it was suspected that catenins might link cadherins to the cytoskeleton. α-catenin β-catenin δ-catenin γ-catenin All but α-catenin contain armadillo repeats. Several types of catenins work with N-cadherins to play an important role in learning and memory (For full article, see Cadherin-catenin complex in learning and memory). Cell-cell adhesion complexes are required for simple epithelia in higher organisms to maintain structure, function and polarity. These complexes, which help regulate cell growth in addition to creating and ...
In multi-cellular organisms, cell-cell contacts that are mediated by classical cadherins have essential roles in many fundamental processes, such as morphogenesis, maintenance of tissue integrity, wound healing and cell polarity. Furthermore, there is overwhelming evidence that the adherens junctions (AJs) are also an important tumor and/or invasion suppressor. Alpha-catenin is the protein that connects E-cadherin-beta-catenin complexes with the actin cytoskeleton. Although it was previously considered to be a solely structural protein, it has become increasingly clear that alpha-catenin has a central role in both assembling the actin cytoskeleton and regulating its dynamics at cell-cell junctions thus regulating cell polarity. Cell-polarity mechanisms are responsible not only for the diversification of cell shapes but also for regulation of the asymmetric cell divisions of stem cells that are crucial for their correct self-renewal and differentiation. Disruption of cell polarity is a hallmark ...
In multi-cellular organisms, cell-cell contacts that are mediated by classical cadherins have essential roles in many fundamental processes, such as morphogenesis, maintenance of tissue integrity, wound healing and cell polarity. Furthermore, there is overwhelming evidence that the adherens junctions (AJs) are also an important tumor and/or invasion suppressor. Alpha-catenin is the protein that connects E-cadherin-beta-catenin complexes with the actin cytoskeleton. Although it was previously considered to be a solely structural protein, it has become increasingly clear that alpha-catenin has a central role in both assembling the actin cytoskeleton and regulating its dynamics at cell-cell junctions thus regulating cell polarity. Cell-polarity mechanisms are responsible not only for the diversification of cell shapes but also for regulation of the asymmetric cell divisions of stem cells that are crucial for their correct self-renewal and differentiation. Disruption of cell polarity is a hallmark ...
3.0.CO;2-R. PMID 8806074. Sheikh F, Chen Y, Chen Y, Liang X, Hirschy A, Stenbit AE, Gu Y, Dalton ND, Yajima T, Lu Y, Knowlton KU, Peterson KL, Perriard JC, Chen J (Sep 2006). "alpha-E-catenin inactivation disrupts the cardiomyocyte adherens junction, resulting in cardiomyopathy and susceptibility to wall rupture". Circulation. 114 (10): 1046-55. doi:10.1161/CIRCULATIONAHA.106.634469. PMID 16923756. Su LK, Vogelstein B, Kinzler KW (December 1993). "Association of the APC tumor suppressor protein with catenins". Science. 262 (5140): 1734-7. doi:10.1126/science.8259519. PMID 8259519. Daniel JM, Reynolds AB (September 1995). "The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin". Mol. Cell. Biol. 15 (9): 4819-24. doi:10.1128/mcb.15.9.4819. PMC 230726 . PMID 7651399. Oyama T, Kanai Y, Ochiai A, Akimoto S, Oda T, Yanagihara K, Nagafuchi A, Tsukita S, Shibamoto S, Ito F (December 1994). "A truncated beta-catenin disrupts ...
Wnt pathway deregulation is a common characteristic of many cancers. But only Colorectal Cancer predominantly harbours mutations in APC, whereas other cancer types (hepatocellular carcinoma, solid pseudopapillary tumours of pancreas) have activating mutations in β-catenin (CTNNB1). We have compared the dynamics and the potency of β-catenin mutations in vivo. Within the murine small intestine (SI), an activating mutation of β-catenin took much longer to achieve a Wnt deregulation and acquire a crypt-progenitor-cell (CPC) phenotype than Apc or Gsk3 loss. Within the colon, a single activating mutation of β-catenin was unable to drive Wnt deregulation or induce the CPC phenotype. This ability of β-catenin mutation to differentially transform the SI versus the colon correlated with significantly higher expression of the β-catenin binding partner E-cadherin. This increased expression is associated with a higher number of E-cadherin:β-catenin complexes at the membrane. Reduction of E-cadherin ...
Our understanding of the role of WNT/β-catenin signalling in melanoma continues to evolve. In mouse models, activating WNT/β-catenin signalling using a melanocyte-specific, constitutively active β-catenin is by itself not sufficient to promote spontaneous melanoma tumourigenesis (Damsky et al, 2011; Delmas et al, 2007). However, constitutively active β-catenin promotes melanoma tumour initiation in the background of a mutant active Nras (Delmas et al, 2007). Knocking out β-catenin similarly inhibits melanoma tumourigenesis in mice carrying Braf and Pten mutations (Damsky et al, 2011). In contrast, our previous results using established murine and human melanoma cell lines indicate that activating WNT/ß-catenin signalling with WNT3A can inhibit the growth of melanoma cells in vitro and in vivo (Biechele et al, 2012; Chien et al, 2009b). Another recent study finds that either activating WNT/β-catenin signalling with a constitutively active β-catenin or knocking out β-catenin disrupts ...
In metazoan adherens junctions, β-catenin links the cytoplasmic tail of classical cadherins to the F-actin-binding protein α-catenin. Phosphorylation of a Ser/Thr-rich region in the cadherin tail dramatically enhances affinity for β-catenin and promotes cell-cell adhesion in cell culture systems, but its importance has not been demonstrated in vivo. In this paper, we identify a critical phosphorylated serine in the C. elegans cadherin HMR-1 required for strong binding to the β-catenin homolog HMP-2. Ablation of this phosphoserine interaction produces developmental defects that resemble full loss-of-function (Hammerhead and Humpback) phenotypes. Most metazoans possess a single gene for β-catenin, which is also a transcriptional coactivator in Wnt signaling. Nematodes and planaria, however, have a set of paralogous β-catenins; for example, C. elegans HMP-2 functions only in cell-cell adhesion, whereas SYS-1 mediates transcriptional activation through interactions with POP-1/Tcf. Finally, our ...
Several studies have shown that β‐catenin levels increase upon Wg/Wnt signaling (Miller and Moon, 1996; Yost et al., 1996; Young et al., 1998). Here, we have investigated whether this increased half‐life sets the threshold for signaling. Using ALLN and ts20 cells, we demonstrate that signaling by β‐catenin/TCF is not a direct consequence of the increased β‐catenin half‐life that occurs upon Wnt signaling. Rather, the data suggest that changes in the phosphorylation status of the N‐terminus of β‐catenin that occur upon Wnt signaling independently affect the signaling properties and half‐life of β‐catenin. Using a monoclonal antibody (αABC) directed against dephosphorylated β‐catenin, we show that only bona fide Wnt signals lead to an increase in unphosphorylated β‐catenin.. We noticed that the increase in TCF‐mediated transcription for LiCl treatment is far greater than the increase in the active form of β‐catenin, whereas Wnt1 transfection results in a modest ...
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Nasopharyngeal carcinoma has a high incidence in southern China. The Wnt/β-catenin signaling pathway plays a major role in cancer development and progression. Our current study aims to determine the clinical significance of the Wnt/β-catenin pathway components such as β-catenin, cyclooxygenase 2, cyclin D1, c-Myc, and E-cadherin in 148 nasopharyngeal carcinomas by immunohistochemistry. We found that nasopharyngeal carcinoma stage T3+T4 had significantly higher expression of β-catenin, cyclooxygenase 2, cyclin D1, and c-Myc and lower expression of E-cadherin than nasopharyngeal carcinoma stage T1+T2 (P | .001, P | .05, respectively).There was significantly higher expression of β-catenin (P = .001) and cyclooxygenase 2 (P = .003) and lower expression of E-cadherin (P = .001) in nasopharyngeal carcinoma with lymph node metastasis than in nasopharyngeal carcinoma without lymph node metastasis. The expression of β-catenin in nasopharyngeal carcinoma was positively correlated with cyclooxygenase 2 (r =
The present study demonstrated and confirmed the expression of several important molecules in canine OSA, showing a potential prognostic value of some of them, that could also be considered as possible candidates for a therapeutic target.. Even though the importance of the Wnt/β-catenin pathway in bone development and homeostasis is well defined [46, 47], the role of β-catenin in the development and progression of bone tumours is not completely known [48]. Since OSA formation is probably the result of an altered bone regulation, it seems likely that deregulation of the Wnt signalling could be associated with the pathogenesis of OSA. The presence of intense β-catenin-positive nuclei in normal osteoblasts observed in the present study would confirm the fundamental role of the Wnt/β-catenin pathway in the maintenance of these cells. Indeed, nuclear β-catenin expression has been considered a hallmark of activation of the Wnt/β-catenin pathway [26, 49] or mutations of β-catenin or molecules of ...
Pancreatic β-cells are highly responsive to changes in glucose, but the mechanisms involved are only partially understood. There is increasing evidence that the β-catenin signalling pathway plays an important role in regulating β-cell function, but the mechanisms regulating β-catenin signalling in these cells is not well understood. In the present study we show that β-catenin levels and downstream signalling are regulated by changes in glucose levels in INS-1E and β-TC6-F7 β-cell models. We found a glucose-dependent increase in levels of β-catenin in the cytoplasm and nucleus of INS-1E cells. Expression of cyclin D1 also increased with glucose and required the presence of β-catenin. This was associated with an increase in phosphorylation of β-catenin on Ser552, which is known to stabilize the molecule and increase its transcriptional activity. In a search for possible signalling intermediates we found forskolin and cell-permeable cAMP analogues recapitulated the glucose effects, ...
Calcium-dependent homotypic cell-cell adhesion, mediated by molecules such as E-cadherin, guides the establishment of classical epithelial cell polarity and contributes to the control of migration, growth, and differentiation. These actions involve additional proteins, including alpha- and beta-catenin (or plakoglobin) and p120, as well as linkage to the cortical actin cytoskeleton. The molecular basis for these interactions and their hierarchy of interaction remain controversial. We demonstrate a direct interaction between F-actin and alpha (E)-catenin, an activity not shared by either the cytoplasmic domain of E-cadherin or beta-catenin. Sedimentation assays and direct visualization by transmission electron microscopy reveal that alpha 1(E)-catenin binds and bundles F-actin in vitro with micromolar affinity at a catenin/G-actin monomer ratio of approximately 1:7 (mol/mol). Recombinant human beta-catenin can simultaneously bind to the alpha-catenin/actin complex but does not bind actin ...
The adherens junction (AJ) comprises protein complexes involved in cell-cell adhesion and collective cell migration in embryonic development (Halbleib and Nelson, 2006). Cell-cell adhesion at the AJ is mediated by classical cadherins, such as E-cadherin, via trans interactions between their extracellular domains on opposing cells (Stemmler, 2008). The cytoplasmic domain of classical cadherins binds β-catenin and p120-catenin (Shapiro and Weis, 2009), and β-catenin in turn binds the actin-binding protein α-catenin that connects the AJ with the actin cytoskeleton (Benjamin and Nelson, 2008). α-Catenin might have additional roles in cell polarity, signal transduction and as a tension transducer (Gladden et al., 2010; Yonemura et al., 2010; Schlegelmilch et al., 2011).. Early models proposed that vertebrate α-catenin provides a static bridge between the AJ and the actin cytoskeleton (Rimm et al., 1995). However, recent studies have caused a re-evaluation of α-catenin regulation and function. ...
Clone REA548 recognizes the S879-phosphorylated form of p120 catenin, a prototypic member of the subfamily of armadillo-domain (ARM) proteins. p120 ARM domain displays 22% homology to other ARM-domain proteins such as β-catenin and plakoglobin, which are basically cadherin binding proteins, suggesting the involvement of p120 in binding to cadherin. p120 associates with most classical (type I) and non-classical (type II) cadherins via ARM repeats 1-7 and is localised at the cell junctions, where it constitutes the cadherin complex. Functions of p120 include regulation of stability of cadherins and modulation of activity of rho GTPases in the cytoplasm. Furthermore, lack of p120 catenin in mouse leads to tumor development, suggesting its further role as tumor supressor. Phosphorylation of p120 catenin at multiple sites regulates its various functions and can be phosphorylated by Src and various receptor tyrosine kinases. Additional information: Clone REA548 displays negligible binding to Fc receptors. -
Clone REA548 recognizes the S879-phosphorylated form of p120 catenin, a prototypic member of the subfamily of armadillo-domain (ARM) proteins. p120 ARM domain displays 22% homology to other ARM-domain proteins such as β-catenin and plakoglobin, which are basically cadherin binding proteins, suggesting the involvement of p120 in binding to cadherin. p120 associates with most classical (type I) and non-classical (type II) cadherins via ARM repeats 1-7 and is localised at the cell junctions, where it constitutes the cadherin complex. Functions of p120 include regulation of stability of cadherins and modulation of activity of rho GTPases in the cytoplasm. Furthermore, lack of p120 catenin in mouse leads to tumor development, suggesting its further role as tumor supressor. Phosphorylation of p120 catenin at multiple sites regulates its various functions and can be phosphorylated by Src and various receptor tyrosine kinases. Additional information: Clone REA548 displays negligible binding to Fc receptors. -
The transcriptional coactivator Yap, a downstream effector of the Hippo signaling pathway, was shown recently to be necessary and sufficient for cardiomyocyte proliferation.19,20 Moreover, cardiac-specific expression of activated Yap (eg, αMHC-YapS112A) that cannot be phosphorylated by inhibitory upstream kinases in the Hippo pathway enhances cardiac regeneration post MI.22,23 However, the upstream regulators that control Yap activity in the heart remain largely unknown. In the present study, we demonstrate that depletion of αE- and αT-catenin in the postnatal heart leads to nuclear accumulation of Yap and induction of cardiomyocyte proliferation. Importantly, deletion of both α-catenin genes in adult heart before injury (IN-DKO model) led to improved cardiac function compared with control littermates. A 2-fold increase in nuclear Yap in cardiomyocytes of the injured IN-DKO relative to WT hearts suggests that Yap transcriptional activity likely contributes to the enhanced cardiomyocyte ...
In cells not exposed to the signal, β-catenin levels are kept low through interactions with the protein kinase zw3/GSK-3, CK1a, APC and Axin (Behrens, 1998 Itoh 1998., Hamada, 1999.) β-catenin is degraded, after phosphorylation by GSK-3 and CK1 alpha (Yanagawa 2002, Liu 2002, Amit 2002), through the ubiquitin pathway (Aberle 1997.), involving interactions with Slimb/bTrCP (Jiang 1998, Marikawa 1998,; reviewed in Maniatis 1999). In a current model, Wnt signaling initially leads to a complex between Dsh, GBP/Frat1, Axin and Zw3/GSK, which may be the regulatory step in the inactivation of Zw3/GSK (Salic, 2000; Farr 2000). The DIX domain in Axin is similar to the NH2 terminus in Dsh, and promotes interactions between Dsh and Axin (Hsu 1999, Smalley, 1999). As a consequence, GSK does not phosphorylate β-catenin anymore, releasing it from the Axin complex and accumulation (Salic, 2000).The stabilized β-catenin then enters the nucleus to interact with TCF. β-catenin can convert TCF into a ...
The most cogent studies supporting the S45 primer model used exogenously overexpressed β-catenin mutants and did not examine cells of intestinal epithelial origin, the major cell type in which disruption of this pathway results in neoplasia. We reasoned that naturally occurring mutations of the β-catenin gene in colorectal cancers could provide a unique opportunity to address this model in cells of colorectal epithelial origin under near physiological conditions (i.e., without overexpression of exogenous proteins). It was reported previously that the colorectal cancer cell line LS 174T harbors a mutation of β-catenin at codon 45 (S45F). We confirmed the presence of the S45F mutation in LS 174T and further determined that these cells lacked a WT 3 allele (Fig. 1A) ⇓ . Accordingly, the S45 primer model would suggest that phosphorylation of β-catenin at S33, S37, or T41 should be absent or greatly diminished in these cells. Indeed, previous studies using overexpressed mutant S45F β-catenin ...
The present study identified five new β-catenin target genes in thalamic neurons, in addition to previously described Cacna1g[16]. Three of them, Kcna6, Calb2, and Gabra3, were validated by ChIP in vivo and a loss-of-function experiment in cultured neurons, confirming that they might be directly regulated by β-catenin. Two other genes, Cacna2d2 and Kcnh8, also displayed β-catenin-dependence in the latter experiment, although the binding of β-catenin to their regulatory elements was not found. Based on these data, we propose that β-catenin is a regulator of the electrophysiological properties of thalamic neurons in the adult brain.. Numerous genes that we selected in silico as potentially regulated by β-catenin belong to expected functional categories: transcription regulation, cell proliferation, morphogenesis, motility, adhesion, differentiation, and programmed cell death. Similar clusters were observed by others in the genes bound by TCF7L2 in a human colorectal cancer cell line [40]. ...
Results We found that five SNPs in the introns of MEF2C were associated with forearm BMD at a genome-wide significance level (p,5×10-8) in meta-analysis (lead SNP, rs11951031[T] −0.20 SDs per allele, p=9.01×10-9). The gene-based association test suggested an association between MEF2C and forearm BMD (p=0.003). The association between MEF2C variants and risk of fracture did not achieve statistical significance (SNP rs12521522[A]: OR=1.14 (95% CI 0.92 to 1.35), p=0.14). Meta-analysis also revealed two genome-wide suggestive loci at CTNNA2 and 6q23.2.. ...
Arteriogenesis requires smooth muscle cell (SMC) investment of endothelial tubes to build the arterial wall. In preliminary studies in mice, inactivation of SMC β-catenin, a downstream mediator of canonical Wnt signaling and a key element of the structural cadherin-catenin complex, caused embryonic demise with apparent vascular enlargement and hemorrhage. In detailed analysis, we found that SMC β-catenin is required for arteriogenesis: embryos lacking SMC β-catenin (SMKO) died by E12.5 (93 embryos and 215 pups analyzed) with impaired arterial maturation, with thinner aortic walls by E10.5 (SMKO vs. WT p,0.0001, n=8) due to impaired SMC investment, decreased cell proliferation (E9.5 to E11.5 SMKO vs. WT p5), and increased apoptosis (E11.5 SMKO n=11 vs. WT n=18, p,0.05). Interestingly, β-catenin-deficient SMCs had impaired growth and survival and increased p53 activity, though p53 levels were unchanged. In vivo, SMC p53 inactivation suppressed phenotypes caused by loss of β-catenin: at E12.5, ...
β-Catenin expression was observed in the membrane and/or cytoplasm without any significant nuclear expression. HER-2/neu and EGFR were observed on the membrane in 21% and 6% of tumors, respectively, and Met stained in a membrane/cytoplasm distribution in 28% of cases. Cyclin D1 was expressed in the nucleus and MMP7 was expressed in the cytoplasm in 26% and 75% of tumors, respectively. Nuclear expression of p53 was noted in 31% of tumors. When each marker was analyzed separately, only p53 and Met demonstrated a significant correlation with survival. However, patients who had tumors that coexpressed high levels of β-catenin and p53 had markedly worse overall survival (P = 0.0026). In multivariate analysis, only tumor size, Met, and the coexpression of β-catenin and p53 retained statistical significance. ...
The Wnt/β-catenin pathway regulates the cell growth and survival following radiation in various types of cancer cells. Our previous report show that activation of the Wnt/β-catenin signaling pathway is a key radioprotective mechanism in irradiated head and neck cancer (HNC) cells. However, the molecular mechanisms by which β-catenin regulates radiation sensitivity are not clear. Here we attempted to elucidate the mechanism of cell death following radiation by studying how β-catenin silencing controls the radiation sensitivity of radioresistant HNC cells.. Of nine cell lines examined, the most radioresistant cell line (AMC-HN-9) were selected for this experiments. β-catenin silencing using small interfering RNA(siRNA) down-regulated β-catenin expression up to 72 h, which was confirmed by western blot analysis. The sensitivity to radiation was anlayzed by clonogenic analysis and MTT assay. As a result, β-catenin silencing remarkably decreased the survival of irradiated AMC-HN-9 cells and ...
Shop Juxtamembrane domain-associated catenin ELISA Kit, Recombinant Protein and Juxtamembrane domain-associated catenin Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Cadherins are transmembrane glycoproteins vital in calcium-dependent cell-cell adhesion during tissue differentiation. Cadherins cluster to form foci of homophilic binding units. A key determinant to the strength of the cadherin-mediated adhesion may be by the juxtamembrane region in cadherins. This region induces clus
A synthetic peptide corresponding to a sequence at the C-terminus of human beta Catenin(764-781aa DGLPPGDSNQLAWFDTDL), identical to the related rat and mouse and zebrafish sequences. ...
Rabbit polyclonal beta Catenin (phospho Y489) antibody validated for WB, ICC and tested in Human. Immunogen corresponding to synthetic peptide
Rabbit polyclonal gamma Catenin (phospho Y550) antibody validated for WB, ELISA and tested in Human, Mouse and Rat. Immunogen corresponding to synthetic peptide
Adhesion to the extracellular matrix (ECM) or to neighboring cells regulates multiple cellular processes such as cell migration, morphogenesis, proliferation, gene expression and survival. Activation and regulation of these responses depends on multiple environmental cues, which are sensed and interpreted in specific cell-matrix and cell-cell adhesions. In our lab, we focus in particular on integrin- and cadherin-mediated adhesions, and study the mechanisms whereby they sense external surfaces, recognizing not only their chemical composition, but also their physical properties, including their topography, rigidity and ligand density. Systematic molecular modulation of the adhesion sites is used in an attempt to decipher the mechanisms whereby the adhesion-based molecular machinery integrates complex environmental information and triggers a coherent and robust response. Specifically, we combine a wide variety of molecular perturbation approaches with advanced, quantitative imaging technologies, ...
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Tony Sirico ("The Sopranos") and Morgan Fairchild will star in the Texas-based indie comedy "The Sno Cone Stand, Inc." says Reuters.. Writer-director-producer Travis Knapp created the film about three stockbroker trainees who hate their jobs and self-absorbed boss Mr. Bob (Sirico) and try to get rich quick by launching a snow cone business.. Fairchild will play Mr. Bobs sales manager. Filming is slated to begin September 4th in Austin.. ...
BACKGROUND. To the authors knowledge, little is known regarding the role of E-cadherin/β-catenin system dysregulation in pulmonary neuroendocrine tumors. METHODS. E-cadherin and β-catenin immunoreactivity was evaluated in 10 hyperplastic neuroendocrine tumorlets and 210 neuroendocrine tumors, including 96 typical carcinoids (CTs), 35 atypical carcinoids (ACTs), 49 large cell neuroendocrine carcinomas (LCNECs), and 30 small cell lung carcinomas (SCLCs). RESULTS. Normal and hyperplastic bronchial neuroendocrine cells expressed E-cadherin/β-catenin with an orderly distribution along the cell membrane. Neuroendocrine tumors retained β-catenin expression in all tumors and E-cadherin in most tumors, with the exception of 2% of LCNECs, 3% of SCLCs and 9% of ACTs. E-cadherin showed a prevalent membrane-associated, linear immunoreactivity in CTs, whereas membrane-disarrayed and cytoplasmic staining was seen in most ACTs, LCNECs, and SCLCs (P , 0.001). β-Catenin exhibited similar immunoreactivity ...
Thymic epithelial tumors (TET) are rare. Wingless and INT (WNT), NOTCH and sonic hedgehog pathway interactions between thymocytes and thymic stroma are important to thymus and T-cell development. We analyzed a thymoma tissue microarray (TMA) for glioma associated oncogene homolog 1 (GLI1), NOTCH1 and catenin (cadherin-associated protein, beta 1) (CTNNB1) expression as surrogate markers of sonic hedgehog, NOTCH and WNT pathway activity.GLI1, NOTCH1 and CTNNB1 expression were assayed in a tissue microarray of 68 TET and eight benign thymus by fluorescent immunohistochemistry (AQUA) as surrogates for activity of the sonic hedgehog, NOTCH and WNT pathways respectively.No difference in tumor GLI1 (mean 201 vs. 211, p=0.31), CTNNB1 (mean 222 vs. 306, p=0.66) or NOTCH1 expression (mean 317 vs. 325, p=0.82) was noted between thymic tumor and benign thymus.No evidence for preferential expression of GLI1, NOTCH1 or CTNNB1 was noted. High-throughput immunofluorescence using AQUA technology can help ...
Due to alterations of any components in this pathway, Wnt/β-catenin signaling pathway is aberrantly activated in various cancers. β-catenin can also be activated or stabilized by other factors to promote cancer development. For example, long noncoding RNA pancEts-1 accelerates neuroblastoma progression via hnRNPK-mediated stabilization of β-catenin [33]. Cytoplasmic hPCL3s, which is highly expressed in HCC samples, promotes HCC metastasis through activation of β-catenin/IL6 pathway [34]. After stabilizing or activating by Wnt signals or other factors, β-catenin enters the nucleus and elicits its transcriptional activity. The most initially identified targets for β-catenin are c-myc and cyclin D1, which act as oncogenic roles in cancer development. Additionally, Deptor, a suppressor of mTOR, has been demonstrated as a novel target of Wnt/β-catenin/c-Myc signaling pathway and contributes to the growth of colorectal cancer cell [35]. Here, we showed that the expression of β-catenin as well ...
We review evidence concerning the basis for tissue segregation during embryonic development. This compartmentalization is shown to be an immiscibility phenomenon caused by changes in the strengths of adhesions between mobile cells which accompany their differentiation and generate interfacial tensions at cell population boundaries. The mobile cells exchange neighbors in response to these adhesion-generated forces which impel the system toward the configuration of maximal binding. Cadherins dominate these intercellular adhesions, but integrin-fibronectin-based adhesions also contribute to them as well as to cell-matrix adhesions. At the interface between two segregating cell populations are three kinds of cell-cell interfaces: a-a, b-b and a-b. Tissue immiscibility (segregation) results when the cross-adhesion is weaker than the mean value of the two kinds of self-adhesions, does not require (although it permits) qualitative changes in cell adhesion molecules and is easily generated even by
β-catenin, the critical effector of the Wnt pathway, regulates a number of key processes during development including proliferation, differentiation and cell fate determination, as well as tissue homeostasis in adults. β-catenin is normally localized to the cell adhesion junctions in epithelial cells and its abnormal cytplasmic/nuclear stabilization drives uncontrolled transcription of target genes (including c-jun, cyclin D1, c-myc, survivin, and MMP-7) regulating cell proliferation, survival and cell adhesion.12 In view of its biological importance, it is not surprisingly that deregulation of β-catenin has been linked to the pathogenesis of a number of human cancers, particularly those with an epithelial cell origin.28 Illegitimate activation of β-catenin has also been reported in several types of hematopoietic cancers.19,29-31 Nevertheless, the functional status and biological role of β-catenin have never been investigated in ALK+ALCL. In this study, we found that β-catenin is ...
The natural agent rhein is an ananthraquinone derivative of rhubarb, which has anticancer effects. To determine the mechanisms underlying the anticancer effects of rhein, we detected the effect of rhein on several oncoproteins. Here, we show that rhein induces β-catenin degradation in both hepatoma cell HepG2 and cervical cancer cell Hela. Treatment of HepG2 and Hela cells with rhein shortens the half-life of β-catenin. The proteasome inhibitor MG132 blunts the downregulation of β-catenin by rhein. The induction of β-catenin degradation by rhein is dependent on GSK3 but independent of Akt. Treatment of HepG2 and Hela cells with GSK3 inhibitor or GSK3β knockdown abrogates the effect of rhein on β-catenin. GSK3β knockdown compromises the inhibition of HepG2 and Hela cell growth by rhein. Furthermore, rhein dose not downregulate β-catenin mutant that is deficient of phosphorylation at multiple residues including Ser33, Ser37, Thr41 and Ser45. Moreover, rhein induces cell cycle arrest at S ...
To better understand the development of HSCs, we have investigated the role of Wnt/β-catenin signaling in the mouse embryonic aorta in the AGM region at midgestation. The AGM region exhibits activated β-catenin (as well as β-catenin activity) in a small subpopulation of endothelial-like cells. We have demonstrated that embryonic endothelial cells lacking β-catenin activity (by pharmacological inhibition or genetic deletion) preclude their contribution to generate HSCs and contribute to the hematopoiesis of the adult organism.. Wnt canonical pathway is important in the maintenance of several types of stem cells such as intestinal, epidermal, or mammary (Reya and Clevers, 2005); however, some questions still remain about the role of β-catenin for the generation and maintenance of HSCs. It has been shown that activation of β-catenin in BM hematopoietic precursors increases the pool of cells with long-term repopulating capacity (Reya et al., 2003; Willert et al., 2003; Goessling et al., 2009) ...
TY - JOUR. T1 - Expression of cadherins and catenins in paired tumor and non-neoplastic primary prostate cultures and corresponding prostatectomy specimens. AU - Wang, J.. AU - Krill, D.. AU - Torbenson, Michael. AU - Wang, Q.. AU - Bisceglia, M.. AU - Stoner, J.. AU - Thomas, A.. AU - DeFlavia, P.. AU - Dhir, R.. AU - Becich, M. J.. PY - 2000/1/1. Y1 - 2000/1/1. N2 - Cadherins are a family of transmembrane proteins that play a crucial role in cell differentiation, cell migration, and intercellular adhesion. Cadherins are associated with catenins through their highly conserved cytoplasmic domain. Down-regulation of E-cadherin protein has been shown in various human cancers. This study examined the expression of cadherins and associated catenins at the mRNA level. Paired tumor and non-neoplastic primary prostate cultures were obtained from surgical specimens. Quantitative multiplex fluorescence reverse transcriptase-polymerase chain reaction (QMF RT-PCR) and quantitative analysis were performed ...
ARMc8 (armadillo-repeat-containing protein 8) is a key component of the CTLH (C-terminal to lissencephaly type-1-like homology motif) complex in mammalian cells. This complex is well conserved in Saccharomyces cerevisiae and has been characterized as a FBPase (fructose-1, 6-bisphosphatase)-degrading complex. The yeast homologue of ARMc8, Gid (glucose-induced degradation) 5p, plays an essential role in the ubiquitin- and proteasome-dependent degradation of FBPase. To elucidate the function of ARMc8, we used a yeast two-hybrid system to screen a human skeletal muscle cDNA library. α-Catenin was isolated as a binding protein of ARMc8α. This association was confirmed by co-immunoprecipitation assay using MDCK (Madin-Darby canine kidney) cells in which exogenous α-catenin and ARMc8α were overexpressed. The association was also confirmed by co-immunoprecipitation assay using endogenous proteins in untransfected MDCK cells. We then used immunofluorescence microscopy of MDCK cells and C2C12 cells to ...
Results Complete data were available on 19 patients comprising; two polyp cancers, six Dukes A, four Dukes B and seven Dukes C tumours. There were eight right-sided, seven left-sided and four rectal tumours. Higher levels of nuclear β-Catenin staining were noted in the 11 patients with node negative disease (mean H-score = 1.8; SD = 0.4) than in node positive disease (mean H-score = 1.3; SD = 0.2; p = 0.03, Mann-Whitney). Interestingly lower nuclear expression of β-Catenin was seen in the patient with a polyp cancer and node positive disease than in the polyp cancer without nodal disease (H-score 1.4 vs. 2.4). ...
This report characterizes phenotypic alterations that result from β-catenin overexpression in a nontransformed epithelial cell line. Effects are seen in the regulation of three important cellular activities/properties: proliferation, apoptosis, and morphology. It demonstrates that modest β-catenin overexpression significantly enhances the ability of these cells to proliferate, especially in situations that would normally inhibit the cell cycle at the G1/S transition. Most striking is the demonstration that it promotes growth in soft agar, a phenotype closely correlated with tumorigenicity. Most nontransformed cells require adhesion through integrin receptors to extracellular matrix components to transit through the G1 phase of the cell cycle (Mehta et al. 1986; Polyak et al. 1994). In addition, suspension of normal, attachment-dependent cells blocks them late in G1 phase.. β-Catenin overexpression also resulted in increased proliferation of cells at high cell density. The mechanism by which ...
Background: β‐Catenin is an important signaling molecule in the Wnt pathway that plays a key role in tumorgenesis. In the absence of Wnt signaling, the cytoplasmic level of β‐catenin is kept low due to rapid proteasomal‐mediated degradation of GSK3β phosphorylated β‐catenin. Activation of Wnt signaling leads to the inactivation of GSK3β, resulting in stabilization and accumulation of β‐catenin in the cytoplasm. Consequently, β‐catenin translocates into the nucleus, where it binds with members of the T‐cell factor (Tcf)/lymphocyte enhancer‐binding factor family of transcription factors and activates the expression of many target genes important for cancer development. Most colon cancers have activating mutations in the APC tumor suppressor or in β‐catenin itself. Furthermore, activating β‐catenin mutations have been found in a variety of other tumors such as melanomas, hepatocellular carcinomas, skin, breast, and prostate cancer, whereas β‐catenin is not activated ...
When DArcy Wentworth Thompsons On Growth and Form was published 100 years ago, it raised the question of how biological forms arise during development and across evolution. In light of the advances in molecular and cellular biology since then, a succinct modern view of the question states: how do genes encode geometry? Our new special issue is packed with articles that use mathematical and physical approaches to gain insights into cell and tissue patterning, morphogenesis and dynamics, and that provide a physical framework to capture these processes operating across scales.. Read the Editorial by guest editors Thomas Lecuit and L. Mahadevan, as they provide a perspective on the influence of DArcy Thompsons work and an overview of the articles in this issue.. ...
The results of the current study showed the molecular and functional activation of β-catenin by hypoxia in HCC and showed its contribution to hypoxia-induced metastatic phenotypes. The induction of EMT was one of the proinvasive mechanisms augmented by β-catenin during hypoxia. The coexpression of β-catenin and HIF-1α (a marker of hypoxia) in HCC was found to be correlated with metastases and poor prognosis in two independent cohorts of patients. These results confirm the importance of β-catenin in HCC under hypoxic conditions.. Hypoxia plays a critical role in tumor progression (1). Consistent with our previous report (17), it not only facilitated in vitro cell invasion in HCC but also resulted in peritoneal seeding and pulmonary metastasis in an in vivo HAL model. However, the growth of HCC cells and xenografts were suppressed by hypoxia. Further analysis revealed that this could be attributed to the arrest of cell proliferation rather than the induction of apoptosis (Supplementary Fig. ...
View Notes - 2011_Questions_Week_14_Answers from BIO 349 at University of Texas. 1. What happens when you deplete beta catenin in planarians? -The organism is no longer able to form a posterior side
ARMC8_ENST00000491704 Gene, Drug Resistance, Tissue Distribution, Mutation Distribution, Variants, ARMC8_ENST00000491704 Genome Browser, ARMC8_ENST00000491704 References
It has been posited that aspirin treatment may reduce risk for colorectal cancer through inhibition of WNT/cadherin-associated protein β1 (CTNNB1, or β-catenin) signaling. In a study reported recently in the Journal of the National Cancer Institute, Nan et al investigated the potential role of the single nucleotide polymorphism rs6983267 (chromosome 8q24) in the protective effect of aspirin.1 This colorectal cancer susceptibility locus affects binding activity of transcription factor 7 like-2 (TCF7L2) to CTNNB1 and alters expression of target oncogenes, including MYC. The study showed that the T allele of rs6983267 was associated with a protective effect in regular aspirin users and was associated with reduced MYC expression.. The study involved investigation of regular aspirin use and colorectal cancer risk according to genotypes of rs6983267 and CTNNB1 expression in two prospective case-control studies within the Nurses Health Study (women) and the Health Professionals Follow-up Study ...
In addition to its crucial role in cell adhesion, β-catenin is also known to augment gene expression by forming a complex with lymphoid enhancer factor/T-cell factor in the nucleus. Unregulated β-catenin expression and/or its increased nuclear presence can lead to abnormal cell proliferation, tumour invasion and metastasis. Pertinent is the fact that the actin cytoskeleton is central to the translocation of several nuclear proteins. This study investigated whether the actin cytoskeleton influences the nuclear translocation of β-catenin in human oesophageal squamous cell carcinoma (HOSCC), a metastatic disease of common occurrence in South Africa. Disruption of the actin cytoskeleton of five moderately differentiated HOSCC cell lines, with cytochalasin D (cytoD), showed that the nuclear β-catenin level was unaltered in SNO, WHCO1 and WHCO5, but decreased in WHCO3 and WHCO6. CytoD treatment did not affect the cytoplasmic/membrane β-catenin level in these cell lines. Further examination of the ...
E-cadherin-mediated cell-cell adhesion is critical for naive pluripotency of cultured mouse embryonic stem cells (mESCs). E-cadherin-depleted mESC fail to downregulate their pluripotency program and are unable to initiate lineage commitment. To further explore the roles of cell adhesion molecules during mESC differentiation, we focused on p120 catenin (p120ctn). Although one key function of p120ctn is to stabilize and regulate cadherin-mediated cell-cell adhesion, it has many additional functions, including regulation of transcription and Rho GTPase activity. Here, we investigated the role of mouse p120ctn in early embryogenesis, mESC pluripotency and early fate determination. In contrast to the E-cadherin-null phenotype, p120ctn-null mESCs remained pluripotent, but their in vitro differentiation was incomplete. In particular, they failed to form cystic embryoid bodies and showed defects in primitive endoderm formation. To pinpoint the underlying mechanism, we undertook a structure-function approach.
Anti-tumor necrosis factor (anti-TNF) drugs are effective against psoriasis, although 20-30% of patients are nonresponders. Few pharmacogenomic studies have been performed to predict the response to anti-TNF drugs in psoriasis. We studied 173 polymorphisms to establish an association with the response to anti-TNF drugs in patients with moderate-to-severe plaque psoriasis (N=144). We evaluated the response using PASI75 at 3, 6 and 12 months. The results of the multivariate analysis showed an association between polymorphisms in PGLYR4, ZNF816A, CTNNA2, IL12B, MAP3K1 and HLA-C genes and the response at 3 months. Besides, the results for polymorphisms in IL12B and MAP3K1 were replicated at 6 months. We also obtained significant results for IL12B polymorphism at 1 year. Moreover, polymorphisms in FCGR2A, HTR2A and CDKAL1 were significant at 6 months. This is the first study to show an association with these polymorphisms. However, these biomarkers should be validated in large-scale studies before ...
Classical cadherins mediate Ca2+-dependent intercellular adhesion and are essential for tissue morphogenesis and maintenance. They are key components of adherens junctions (AJs). In vitro studies in simple epithelial cells indicated an essential role for E-cadherin not only in the formation of AJs but also other intercellular contacts, such as desmosomes and tight junctions. In contrast, in vivo tissue specific knockout studies did not reveal a necessity of E-cadherin in the formation of intercellular junctions, raising the question if classical cadherins are necessary or if other classical cadherins can compensate for the loss of E-cadherin. Therefore, the aim of this thesis was to ask how E-cadherin regulates tight junctions and if E-cadherin has a specific function in the formation of tight junctions. In addition, the question was asked if classical cadherin function is necessary for the formation of other intercellular contacts, such as desmosomes. Using primary keratinocytes as a model for ...
The Mouse Adherens Junctions RT Profiler PCR Array profiles the expression of 84 key genes encoding components, interactors, and regulators of adherens junctions and desmosomes involved in cell cell contacts mediated by cadherins. Adherens junctions occur at adhesion belts linking adjacent epithelial cells or the focal contacts on the lower surface of cultured fibroblasts. Desmosomes are anchoring cell cell junctions, usually formed between 2 epithelial cells and characterized by dense protein plaques. Adherens junctions connect cadherins to actin filaments internally, while desmosomes connect cadherins to intermediate filaments such as keratin and desmin filaments. Besides cadherins, cell surface receptor components of adherens junctions also include desmocollins, desmogleins, nectins, and Notch proteins. Adherens-junction associated proteins, especially the catenins, recruit protein kinases that regulate the cytoskeleton via phosphorylation cascades and G-proteins that directly recruit ...

CTNNA1 - Catenin alpha-1 - Homo sapiens (Human) - CTNNA1 gene & proteinCTNNA1 - Catenin alpha-1 - Homo sapiens (Human) - CTNNA1 gene & protein

Catenin alpha-1Imported. ,p>Information which has been imported from another database using automatic procedures.,/p> ,p>,a ... tr,E5RJP7,E5RJP7_HUMAN Catenin alpha-1 (Fragment) OS=Homo sapiens GN=CTNNA1 PE=1 SV=1 ...
more infohttp://www.uniprot.org/uniprot/E5RJP7

CTNNA1 Gene - GeneCards | CTNA1 Protein | CTNA1 AntibodyCTNNA1 Gene - GeneCards | CTNA1 Protein | CTNA1 Antibody

Catenin Alpha 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene ... Loss of alpha-catenin decreases the strength of single E-cadherin bonds between human cancer cells. (PMID: 19458087) Bajpai S ... catenin adhesion complex together with E-cadherin/CDH1 and beta-catenin/CTNNB1 or gamma-catenin/JUP; the complex is located to ... CTNNA1 (Catenin Alpha 1) is a Protein Coding gene. Diseases associated with CTNNA1 include Macular Dystrophy, Patterned, 2 and ...
more infohttp://www.genecards.org/cgi-bin/carddisp.pl?gene=CTNNA1

Plus itPlus it

2004) Alpha-catenin: at the junction of intercellular adhesion and actin dynamics. Nat Rev Mol Cell Biol 5:614-625. ... The cadherin intracellular domain also binds β-catenin, which binds through α-catenin to the actin cytoskeleton (for review, ... Receptor tethering by catenins. ABP and GRIP form a scaffold that binds GluR2 and GluR3 (Dong et al., 1997; Srivastava et al., ... Notably, β-catenin, like NPRAP, targets S-SCAM to synapses (Nishimura et al., 2002). NPRAP is also found in complexes with NR2A ...
more infohttp://www.jneurosci.org/content/27/32/8505

Catenin - WikipediaCatenin - Wikipedia

Zhang F, Meng F, Li H, Dong Y, Yang W, Han A (September 2011). "Suppression of retinoid X receptor alpha and aberrant β-catenin ... α-catenin β-catenin δ-catenin γ-catenin All but α-catenin contain armadillo repeats. Several types of catenins work with N- ... The first two catenins that were identified became known as α-catenin and β-catenin. A-catenin can bind to β-catenin and can ... B-catenin binds the cytoplasmic domain of some cadherins. Additional catenins such as γ-catenin and δ-catenin have been ...
more infohttps://en.wikipedia.org/wiki/Catenin

KEGG PATHWAY: Adherens junction - Homo sapiens (human)KEGG PATHWAY: Adherens junction - Homo sapiens (human)

... which in turn binds alpha-catenin. Alpha-catenin is associated with F-actin bundles directly and indirectly. The integrity of ... Cadherin may acts as a negative regulator of signaling beta-catenin as it binds beta-catenin at the cell surface and thereby ... Wnt signaling acts as a positive regulator of beta-catenin by inhibiting beta-catenin degradation, which stabilizes beta- ... which leads to dissociation of the cadherin-catenin complex. Integrity of this complex is positively regulated by beta -catenin ...
more infohttp://www.genome.jp/kegg-bin/show_pathway?133837803022751/hsa04520.args

KEGG PATHWAY: Adherens junction - Homo sapiens (human)KEGG PATHWAY: Adherens junction - Homo sapiens (human)

... which in turn binds alpha-catenin. Alpha-catenin is associated with F-actin bundles directly and indirectly. The integrity of ... Cadherin may acts as a negative regulator of signaling beta-catenin as it binds beta-catenin at the cell surface and thereby ... Wnt signaling acts as a positive regulator of beta-catenin by inhibiting beta-catenin degradation, which stabilizes beta- ... which leads to dissociation of the cadherin-catenin complex. Integrity of this complex is positively regulated by beta -catenin ...
more infohttp://www.kegg.jp/kegg-bin/highlight_pathway?scale=1.0&map=hsa04520

Breaking the connection: displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage...Breaking the connection: displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage...

The APC protein and E-cadherin form similar but independent complexes with alpha-catenin, beta-catenin, and plakoglobin. J Biol ... Identification of plakoglobin domains required for association with N-cadherin and alpha-catenin. J Biol Chem. 1995 Aug 25;270( ... Genetic and biochemical dissection of protein linkages in the cadherin-catenin complex. Proc Natl Acad Sci U S A. 1995 May 23; ... Plakoglobin, or an 83-kD homologue distinct from beta-catenin, interacts with E-cadherin and N-cadherin. J Cell Biol. 1992 Aug; ...
more infohttp://pubmedcentralcanada.ca/pmcc/articles/PMC2120955/?lang=en-ca

Institute of Cancer Research Repository -  beta-Catenin pathway activation in breast cancer is associated with triple-negative...Institute of Cancer Research Repository - beta-Catenin pathway activation in breast cancer is associated with triple-negative...

ALPHA-CATENIN; GAMMA-CATENIN; CYCLIN D1; EXPRESSION; CARCINOMAS. Funding Acknowledgement:. Breakthrough Breast Cancer ; ... and to determine whether aberrant beta-catenin expression is driven by CTNNB1 (beta-catenin encoding gene) activating mutations ... beta-Catenin pathway activation in breast cancer is associated with triple-negative phenotype but not with CTNNB1 mutation ... In conclusion, beta-catenin/Wnt pathway activation is preferentially found in triple-negative/basal-like breast carcinomas, is ...
more infohttp://publications.icr.ac.uk/10393/

Pathway Central: Remodeling of Adherens JunctionsPathway Central: Remodeling of Adherens Junctions

Ctnn-Alpha (Catenin-Alpha) binds to Ctnn-Beta and links components of the Adherens Junctions to the Actin cytoskeleton. It also ... The cytoplasmic domain of E-Cadherin associates with cytosolic proteins called Catenins (Alpha, Beta and p120), which in turn ... Alpha-Actinin), which in turn binds to F-Actin. p120Ctn (p120Catenin), another member of the Catenin family, binds to the ... causing the dissociation of Alpha-Ctnn from the Cadherin-Catenin complex and formation of weak adhesions. The level of junction ...
more infohttp://www.sabiosciences.com/pathway.php?sn=Remodeling_of_Adherens_Junctions

Loss of E-cadherin-dependent cell-cell adhesion due to mutation of the beta-catenin gene in a human cancer cell line, HSC-39. |...Loss of E-cadherin-dependent cell-cell adhesion due to mutation of the beta-catenin gene in a human cancer cell line, HSC-39. |...

... alpha-catenin, and gamma-catenin and a 79-kDa band which was apparently smaller than that of normal beta-catenin, indicating ... Southern blotting of beta-catenin DNA disclosed mutation at the genomic level. Expression vectors of Beta-catenin were ... The 79-kDa band was immunologically identified as beta-catenin by using immunoblotting with anti-beta-catenin antibodies. ... Loss of E-cadherin-dependent cell-cell adhesion due to mutation of the beta-catenin gene in a human cancer cell line, HSC-39.. ...
more infohttps://mcb.asm.org/content/15/3/1175?ijkey=eb1e07c6408d5dbddd065c3dc3b8624288d679c3&keytype2=tf_ipsecsha

CTNNB1 catenin (cadherin-associated protein), beta 1 and formation of branching point structures beta-catenin / LEF...CTNNB1 catenin (cadherin-associated protein), beta 1 and formation of branching point structures beta-catenin / LEF...

... catenin) cadherins (the (CDH1) E-cadherin/catenin complex) include the beta-catenins a multifunctional molecule Locus: 3p22.1 ... binds with E-cadherin but not with beta-catenin. Which interacts with (Tcf-T-cell factor where a… ... Catenin Beta 1, CTNNB are cell adhesion molecules called (p120*␠- ... Alpha-catulin may associate with a beta-catenin fraction. In the absence of a Wnt signal, APC normally associates beta-catenin ...
more infohttps://faroucheombre.wordpress.com/2012/03/25/ctnnb1-catenin-cadherin-associated-protein-beta-1-and-formation-of-branching-point-structures-beta-catenin-lef-demonstrating-nucleation-at-tbe1-site-tcf7l2/

Human CTNNA2 qPCR primer pairs | SinoBiologicalHuman CTNNA2 qPCR primer pairs | SinoBiological

Human CTNNA2 qPCR primer pairs, confirmed in positive organizations; screened the primer with high specificity and high sensitivity.
more infohttp://www.sinobiological.com/Human-CTNNA2-qPCR-primer-pairs_p29424.html

Vinculin/alpha-catenin (IPR006077) | InterPro | EMBL-EBIVinculin/alpha-catenin (IPR006077) | InterPro | EMBL-EBI

Alpha-catenins are proteins of about 100 kDa which are evolutionary related to vinculin [PMID: 1924379]. Catenins are proteins ... alpha, beta, and gamma. In terms of their structure the most significant differences are the absence, in alpha-catenin, of the ... The uvomorulin-anchorage protein alpha catenin is a vinculin homologue.. Proc. Natl. Acad. Sci. U.S.A. 88 9156-60 1991 ... The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR006077

Alpha catenin - WikipediaAlpha catenin - Wikipedia

... alpha-2-catenin (also called alpha-N-catenin) alpha-3-catenin (also called alpha-T-catenin) Catenin alpha Catenin at the US ... There are three human alpha-catenin genes: alpha-1-catenin (also called alpha-E-catenin) ... beta-catenin and alpha-catenin has not been isolated. It has been suggested that alpha-catenin does not bind with high affinity ... "Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin". J. Cell Biol. 130 (1): 67 ...
more infohttps://en.wikipedia.org/wiki/Alpha_catenin

Signaling function of alpha-catenin in microtubule regulation.  - PubMed - NCBISignaling function of alpha-catenin in microtubule regulation. - PubMed - NCBI

... cadherins cytoplasmic domain binds p120 catenin and beta-catenin, which in turn binds alpha-catenin. To elucidate the roles of ... plasma membrane targeted or untargeted p120 catenin, alpha-catenin and beta-catenin and tested their ability to rescue the loss ... Right panel represents the scheme of chimeric fusion constructs of α-catenin (A), β-catenin (B) or p120 catenin (C) with either ... Signaling function of alpha-catenin in microtubule regulation.. Shtutman M1, Chausovsky A, Prager-Khoutorsky M, Schiefermeier N ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/18677116?dopt=Abstract

nanoHUB.org - Resources: [Illinois] CMMB IGERT & M-CNTC Annual Symposium: Alpha-Catenin in Cadherin MechanotransductionnanoHUB.org - Resources: [Illinois] CMMB IGERT & M-CNTC Annual Symposium: Alpha-Catenin in Cadherin Mechanotransduction

Home › Online Presentations › [Illinois] CMMB IGERT & M-CNTC Annual Symposium: Alpha-Catenin in Cadherin Mechanotransduction › ... Illinois] CMMB IGERT & M-CNTC Annual Symposium: Alpha-Catenin in Cadherin Mechanotransduction By Hamid Tabdili ... Hamid Tabdili (2013), "[Illinois] CMMB IGERT & M-CNTC Annual Symposium: Alpha-Catenin in Cadherin Mechanotransduction," http:// ...
more infohttp://nanohub.org/resources/14049

Signaling function of alpha-catenin in microtubule regulation. - Semantic ScholarSignaling function of alpha-catenin in microtubule regulation. - Semantic Scholar

... cadherins cytoplasmic domain binds p120 catenin and beta-catenin, which in turn binds alpha-catenin. To elucidate the roles of ... plasma membrane targeted or untargeted p120 catenin, alpha-catenin and beta-catenin and tested their ability to rescue the loss ... Only membrane targeting of alpha-catenin led to a significant increase in microtubule length and density in centrosome-free ... Expression of non-membrane-targeted alpha-catenin produced only a slight effect, while both membrane-targeted and non-targeted ...
more infohttps://www.semanticscholar.org/paper/Signaling-function-of-alpha-catenin-in-microtubule-Shtutman-Chausovsky/85c55b9fb048a403026d0697cb5106c2acf48a39

Catenin alpha Antibodies: Novus BiologicalsCatenin alpha Antibodies: Novus Biologicals

Browse our Catenin alpha Antibody catalog backed by our Guarantee+. ... Catenin alpha Antibodies. We offer Catenin alpha Antibodies for use in common research applications: Immunohistochemistry, ... Our Catenin alpha Antibodies can be used in a variety of model species: Human, Mouse, Xenopus. Use the list below to choose the ... Each Catenin alpha Antibody is fully covered by our Guarantee+, to give you complete peace of mind and the support when you ...
more infohttps://www.novusbio.com/primary-antibodies/catenin-alpha?facet_conjugate=Janelia%20Fluor%20549

Catenin alpha Antibodies: Novus BiologicalsCatenin alpha Antibodies: Novus Biologicals

Browse our Catenin alpha Antibody catalog backed by our Guarantee+. ... Catenin alpha Antibodies. We offer Catenin alpha Antibodies for use in common research applications: Immunohistochemistry, ... Our Catenin alpha Antibodies can be used in a variety of model species: Human, Mouse, Xenopus. Use the list below to choose the ... Each Catenin alpha Antibody is fully covered by our Guarantee+, to give you complete peace of mind and the support when you ...
more infohttps://www.novusbio.com/primary-antibodies/catenin-alpha?facet_conjugate=PE

Catenin alpha-1 - WikipediaCatenin alpha-1 - Wikipedia

αE-catenin, also known as Catenin alpha-1 is a protein that in humans is encoded by the CTNNA1 gene. αE-catenin is highly ... αE-catenin has been shown to interact with: APC, Beta-catenin, CDH1, CDH2, CDH3 Plakoglobin, and VE-cadherin. Alpha catenin ... Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin ... "Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin". J. Cell Biol. 130 (1): 67 ...
more infohttps://en.wikipedia.org/wiki/Catenin_alpha-1

catenin alpha 1 ELISA Kits | Biocompare.comcatenin alpha 1 ELISA Kits | Biocompare.com

Compare catenin alpha 1 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and ... catenin alpha 1 ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a well-established antibody-based tool for ... Mouse/Human/Rat Alpha 1+2 Catenin ELISA Kit (Cell-Based ELISA) ... Your search returned 152 catenin alpha 1 ELISA ELISA Kit across ...
more infohttps://www.biocompare.com/pfu/110627/soids/2-2269458/ELISA_Kit/ELISA_catenin_alpha_1

Alpha-catenin-dependent recruitment of the centrosomal protein CAP350 to adherens junctions allows epithelial cells to acquire...Alpha-catenin-dependent recruitment of the centrosomal protein CAP350 to adherens junctions allows epithelial cells to acquire...

Alpha-catenin-dependent recruitment of the centrosomal protein CAP350 to adherens junctions allows epithelial cells to acquire ... We also uncover a central role of α-catenin in global cytoskeleton remodelling, in which it acts not only on actin but also on ... By two-hybrid screening, we identified a direct interaction of CAP350 with the adhesion protein α-catenin that was further ... Block of epithelial cadherin (E-cadherin)-mediated cell-cell adhesion or α-catenin depletion prevented CAP350 localisation at ...
more infohttps://www.sigmaaldrich.com/catalog/papers/25764135

CTNNA2 - Catenin alpha-2 - Pongo abelii (Sumatran orangutan) - CTNNA2 gene & proteinCTNNA2 - Catenin alpha-2 - Pongo abelii (Sumatran orangutan) - CTNNA2 gene & protein

IPR036723. Alpha-catenin/vinculin-like_sf. IPR001033. Alpha_catenin. IPR030046. CTNNA2. IPR006077. Vinculin/catenin. IPR000633. ... IPR036723. Alpha-catenin/vinculin-like_sf. IPR001033. Alpha_catenin. IPR030046. CTNNA2. IPR006077. Vinculin/catenin. IPR000633. ... Belongs to the vinculin/alpha-catenin family.Curated. Phylogenomic databases. evolutionary genealogy of genes: Non-supervised ... sp,Q5R416,CTNA2_PONAB Catenin alpha-2 OS=Pongo abelii GN=CTNNA2 PE=2 SV=3 ...
more infohttp://www.uniprot.org/uniprot/Q5R416

The presence of alpha-catenin in the VE-cadherin complex is required for efficient transendothelial migration of leukocytesThe presence of alpha-catenin in the VE-cadherin complex is required for efficient transendothelial migration of leukocytes

S27D binds to beta-catenin and dissociates alpha-catenin from beta-catenin. (A) HUVEC lysates were incubated with S27D and pull ... Beta-catenin connects VE-cadherin to alpha-catenin. This VE-cadherin-catenin complex is believed to dynamically control ... Western blot was immunostained for beta-catenin (I.B.), which showed that S27D dissociates beta-catenin from alpha-catenin, but ... Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly. Cell. 2005;123: ...
more infohttp://www.ijbs.com/v05p0695.htm

Assessment of the CTNNA3 gene encoding human alpha T-catenin regarding its involvement in dilated cardiomyopathy.  - PubMed -...Assessment of the CTNNA3 gene encoding human alpha T-catenin regarding its involvement in dilated cardiomyopathy. - PubMed -...

... pointing to a specific function for alpha T-catenin in particular muscle tissues. Like other alpha-catenins, alpha T-catenin ... Alpha T-catenin is a novel member of the alpha-catenin family, which shows most abundant expression in cardiomyocytes and in ... They overlap largely with the boundaries of the CTNNA1 and CTNNAL1 genes encoding alpha E-catenin and alpha-catulin, ... As alpha T-catenin is highly expressed in healthy heart tissue, we have considered CTNNA3 as a candidate disease gene in a ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/12596047?dopt=Abstract
  • For instance, when an epithelial layer is complete and the adherens junctions indicate that the cell is surrounded, β-catenin may play a role in telling the cell to stop proliferating, as there is no room for more cells in the area. (wikipedia.org)
  • While the pathway is very detailed and not completely understood, in general, when Wnt is not present, GSK-3B (a member of the pathway) is able to phosphorylate β-catenin as a result of a complex formation that includes β-catenin, AXIN1, AXIN2, APC (a tumor suppressor gene product), CSNK1A1, and GSK3B. (wikipedia.org)
  • These gene products are important in determining cell fates during normal development and in maintaining homeostasis, or they can lead to de-regulated growth in disorders like cancer by responding to mutations in β-catenin, APC or Axin, each of which can lead to this de-regulated β-catenin level stabilization in cells. (wikipedia.org)
  • At this point, β-catenin becomes a coactivator for TCF and LEF to activate Wnt genes by displacing Groucho and HDAC transcription repressors. (wikipedia.org)
  • On the other hand, when Wnt is present, GSK-3B is displaced from the previously mentioned complex, causing β-catenin to not be phosphorylated, and thus not ubiquitinated. (wikipedia.org)
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