The therapeutic potential of acetyl-lysine and methyl-lysine effector domains
Epigenetic reader domains are protein interaction modules that selectively recognize common post-translational modification on histones and other nuclear proteins such as ε-N-acetylated lysine or methyllysine/arginine residues. Interactions mediated by these effector domains result in the recruitmen...
| Main Authors: | , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
2012
|
| _version_ | 1826288860090335232 |
|---|---|
| author | Brennan, P Filippakopoulos, P Knapp, S |
| author_facet | Brennan, P Filippakopoulos, P Knapp, S |
| author_sort | Brennan, P |
| collection | OXFORD |
| description | Epigenetic reader domains are protein interaction modules that selectively recognize common post-translational modification on histones and other nuclear proteins such as ε-N-acetylated lysine or methyllysine/arginine residues. Interactions mediated by these effector domains result in the recruitment of gene specific transcriptional regulators. This review focusses on reader domains that recognize acetylated and methylated lysine and arginine residues. Bromodomains selectively recognize acetylated lysines residues and inhibitors have recently emerged as promising lead compounds for the treatment of cancer and inflammatory diseases, acting by specifically repressing expression of oncogenes and pro-inflammatory cytokines. Initial inhibitors have also been reported for methyllysine binding domains. Here we review recent development of this emerging target area. © 2012 Elsevier Ltd. All rights reserved. |
| first_indexed | 2024-03-07T02:20:06Z |
| format | Journal article |
| id | oxford-uuid:a39d4668-deea-4646-99ed-45e9dd3ac8a4 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T02:20:06Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | oxford-uuid:a39d4668-deea-4646-99ed-45e9dd3ac8a42022-03-27T02:28:14ZThe therapeutic potential of acetyl-lysine and methyl-lysine effector domainsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:a39d4668-deea-4646-99ed-45e9dd3ac8a4EnglishSymplectic Elements at Oxford2012Brennan, PFilippakopoulos, PKnapp, SEpigenetic reader domains are protein interaction modules that selectively recognize common post-translational modification on histones and other nuclear proteins such as ε-N-acetylated lysine or methyllysine/arginine residues. Interactions mediated by these effector domains result in the recruitment of gene specific transcriptional regulators. This review focusses on reader domains that recognize acetylated and methylated lysine and arginine residues. Bromodomains selectively recognize acetylated lysines residues and inhibitors have recently emerged as promising lead compounds for the treatment of cancer and inflammatory diseases, acting by specifically repressing expression of oncogenes and pro-inflammatory cytokines. Initial inhibitors have also been reported for methyllysine binding domains. Here we review recent development of this emerging target area. © 2012 Elsevier Ltd. All rights reserved. |
| spellingShingle | Brennan, P Filippakopoulos, P Knapp, S The therapeutic potential of acetyl-lysine and methyl-lysine effector domains |
| title | The therapeutic potential of acetyl-lysine and methyl-lysine effector domains |
| title_full | The therapeutic potential of acetyl-lysine and methyl-lysine effector domains |
| title_fullStr | The therapeutic potential of acetyl-lysine and methyl-lysine effector domains |
| title_full_unstemmed | The therapeutic potential of acetyl-lysine and methyl-lysine effector domains |
| title_short | The therapeutic potential of acetyl-lysine and methyl-lysine effector domains |
| title_sort | therapeutic potential of acetyl lysine and methyl lysine effector domains |
| work_keys_str_mv | AT brennanp thetherapeuticpotentialofacetyllysineandmethyllysineeffectordomains AT filippakopoulosp thetherapeuticpotentialofacetyllysineandmethyllysineeffectordomains AT knapps thetherapeuticpotentialofacetyllysineandmethyllysineeffectordomains AT brennanp therapeuticpotentialofacetyllysineandmethyllysineeffectordomains AT filippakopoulosp therapeuticpotentialofacetyllysineandmethyllysineeffectordomains AT knapps therapeuticpotentialofacetyllysineandmethyllysineeffectordomains |