User:Isabela Fonseca de Oliveira Granha/Sandbox 1
From Proteopedia
(Difference between revisions)
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The inhibition of ß-catenin destruction leads to increased levels of the protein in cytoplasm and its translocation into the nucleus. ß-catenin interacts with different nuclear pore complex components and ARM repeats <scene name='84/848919/R10-12/1'>R10-R12</scene> are crucial for its import and export. [[Forkhead box protein|FoxM1]] also facilitates its nuclear translocation directly interacting with ARM repeats <scene name='84/848919/R11-12/2'>R11-R12</scene>. [[Forkhead box protein|FoxM1]] forms a complex with ß-catenin/TCF on the promoters of Wnt target genes. Once in the nucleus, ß-catenin and its DNA binding partners can activate transcription of Wnt/ß-catenin target genes. Therefore, ß-catenin can only initiates transcription in a multimeric complex, as its central transcriptional activator. <ref name="valenta2012" /> | The inhibition of ß-catenin destruction leads to increased levels of the protein in cytoplasm and its translocation into the nucleus. ß-catenin interacts with different nuclear pore complex components and ARM repeats <scene name='84/848919/R10-12/1'>R10-R12</scene> are crucial for its import and export. [[Forkhead box protein|FoxM1]] also facilitates its nuclear translocation directly interacting with ARM repeats <scene name='84/848919/R11-12/2'>R11-R12</scene>. [[Forkhead box protein|FoxM1]] forms a complex with ß-catenin/TCF on the promoters of Wnt target genes. Once in the nucleus, ß-catenin and its DNA binding partners can activate transcription of Wnt/ß-catenin target genes. Therefore, ß-catenin can only initiates transcription in a multimeric complex, as its central transcriptional activator. <ref name="valenta2012" /> | ||
- | TCF transcription factors serve as the main nuclear member of ß-catenin multimeric complex. TCFs bind to DNA enhancers and ß-catenin acts as a link in a chain between them and others transcriptional coactivators. This interaction can be modulated to enhance, repress os switch off ß-catenin-mediated transcription. The majority of these transcription coactivators binds to <scene name='84/848919/R12andhelix-c/1'>the last ARM repeat and interacts with Helix-C</scene> and many of them can affect chromatin structure. Indeed, it seems that the C-terminus region of ß-catenin coordinates the recruitment and sequential exchange of these proteins. Binding of ß-catenin to TCF is blocked by some proteins such as<scene name='84/848919/Icat_bcat/2'>ICAT, which interacts with the central ARM repeat of ß-catenin.</scene> <ref name="valenta2012" /> | + | TCF transcription factors serve as the main nuclear member of ß-catenin multimeric complex. TCFs bind to DNA enhancers and ß-catenin acts as a link in a chain between them and others transcriptional coactivators. This interaction can be modulated to enhance, repress os switch off ß-catenin-mediated transcription. The majority of these transcription coactivators binds to <scene name='84/848919/R12andhelix-c/1'>the last ARM repeat and interacts with Helix-C</scene> and many of them can affect chromatin structure. Indeed, it seems that the C-terminus region of ß-catenin coordinates the recruitment and sequential exchange of these proteins. Binding of ß-catenin to TCF is blocked by some proteins such as <scene name='84/848919/Icat_bcat/2'>ICAT, which interacts with the central ARM repeat of ß-catenin.</scene> <ref name="valenta2012" /> |
== References == | == References == | ||
<references/> | <references/> |
Revision as of 17:13, 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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