User:Isabela Fonseca de Oliveira Granha/Sandbox 1
From Proteopedia
(Difference between revisions)
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In the absence of Wnt stimulus, the ß-catenin is located at the cytoplasmic side of the membrane as a component of cadherin-based cell-cell connections. [[Cadherin|Cadherins]] are transmembrane glycoproteins calcium-dependent adhesion that can link to ß-catenin through their cytoplasmic tails. The cadherin-catenin complex forms adherens junctions that polarize epithelial tissues and hold the cells together. <ref>Developmental Biology . Eleventh Edition. By Scott F. Gilbert and Michael J. F. Barresi. Sunderland (Massachusetts): Sinauer Associates. ISBN: 978-1-60535-470-5. 2016. </ref> | In the absence of Wnt stimulus, the ß-catenin is located at the cytoplasmic side of the membrane as a component of cadherin-based cell-cell connections. [[Cadherin|Cadherins]] are transmembrane glycoproteins calcium-dependent adhesion that can link to ß-catenin through their cytoplasmic tails. The cadherin-catenin complex forms adherens junctions that polarize epithelial tissues and hold the cells together. <ref>Developmental Biology . Eleventh Edition. By Scott F. Gilbert and Michael J. F. Barresi. Sunderland (Massachusetts): Sinauer Associates. ISBN: 978-1-60535-470-5. 2016. </ref> | ||
- | The most known interaction occurs between ß-catenin and [[Cadherin|E-cadherin]] (epithelial cadherin). They are associated while still in the endoplasmic reticulum and interfering with the binding of these proteins results in proteasomal degradation of the [[cadherin]]. First, alpha-catenin binds to ß-catenin at the first ARM repeat, <scene name='84/848919/Am118-149/1'>amino acids 118-149</scene>, resulting in an alpha-catenin/ß-catenin heterodimer. This binding stabilizes ß-catenin in the hinged form, and E-cadherin can connect simultaneously. The interaction surface is extensive, covering the entire length of the ß-catenin ARM repeat domain and involving the C-terminal 100 residues of the cadherin cytoplasmic domain. <ref name="valenta2012">DOI 10.1038/emboj.2012.150</ref> <ref name="huber2001">Huber, A. H., & Weis, W. I. (2001). The structure of the β-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by β-catenin. Cell, 105(3), 391-402.</ref> | + | The most known interaction occurs between <scene name='84/848919/Beta-catenin_e-cadherin/1'>ß-catenin and E-cadherin</scene>ß-catenin and [[Cadherin|E-cadherin]] (epithelial cadherin). They are associated while still in the endoplasmic reticulum and interfering with the binding of these proteins results in proteasomal degradation of the [[cadherin]]. First, alpha-catenin binds to ß-catenin at the first ARM repeat, <scene name='84/848919/Am118-149/1'>amino acids 118-149</scene>, resulting in an alpha-catenin/ß-catenin heterodimer. This binding stabilizes ß-catenin in the hinged form, and E-cadherin can connect simultaneously. The interaction surface is extensive, covering the entire length of the ß-catenin ARM repeat domain and involving the C-terminal 100 residues of the cadherin cytoplasmic domain. <ref name="valenta2012">DOI 10.1038/emboj.2012.150</ref> <ref name="huber2001">Huber, A. H., & Weis, W. I. (2001). The structure of the β-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by β-catenin. Cell, 105(3), 391-402.</ref> |
==The ß-catenin destruction complex== | ==The ß-catenin destruction complex== |
Revision as of 16:45, 18 June 2020
ß-catenin
ß-catenin plays essential role in cell adherens junctions - connecting cytoplasmic domains and actin cytoskeleton - and in the canonical Wnt pathway - related to embryonic development. Deregulation of this protein activity is associated with cancer and other diseases, for example, the upregulation of its transcriptional activity is stimulated in most colon cancers. Therefore, ß-catenin is an important target for developing treatment for multiple diseases, with considerable interest in its structure. [1]
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