At the crossroads of SUMO and NF-κB
<p>Abstract</p> <p>Background</p> <p>Recognition of pathogens by immune receptors leads to activation of macrophages, dendritic cells, and lymphocytes. Signals are communicated to enhance expression of target molecules such as cytokines and adhesion molecules, depending...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
BMC
2003-11-01
|
| Series: | Molecular Cancer |
| Subjects: | |
| Online Access: | http://www.molecular-cancer.com/content/2/1/39 |
| _version_ | 1819181221655085056 |
|---|---|
| author | Schmidt Christian Kracklauer Martin P |
| author_facet | Schmidt Christian Kracklauer Martin P |
| author_sort | Schmidt Christian |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>Recognition of pathogens by immune receptors leads to activation of macrophages, dendritic cells, and lymphocytes. Signals are communicated to enhance expression of target molecules such as cytokines and adhesion molecules, depending on activation of various inducible transcription factors, among which the family NF-κB transcription factors plays an evolutionarily conserved and critical role. Classical activation of NF-κB involves phosphorylation, polyubiquitination and subsequent degradation of the inhibitor molecules of NF-κB, referred to as IκB. Modification of IκBα, one of the mammalian IκB isoforms, with the small ubiquitin-like modifier (SUMO) results its protection from degradation.</p> <p>Presentation of the hypothesis</p> <p>SUMO-IκBα localizes in the nucleus. The nuclear SUMO-IκBα pool may be dynamic. SUMO-IκBα functions as synergy control factor.</p> <p>Testing the hypothesis</p> <p>Immunoprecipitation from cellular fractions, <sup>35</sup>S methionine pulse-chase, and FRET assays should reveal the localization of SUMO-IκBα and the dynamics of the pool. Expression of SUMOylation defective IκBα in an <it>IκBα </it><sup>-/- </sup>background should yield insights into the function of SUMO-IκBα.</p> <p>Implication of the hypothesis</p> <p>IκBα contains the required SUMOylation motif but IκBβ does not. The suggested study would provide evidence whether or not IκBα and IκBβ can substitute each other. In addition, the suggested assays would reveal a possible redundancy in controlling transcriptional activity of NF-κB.</p> |
| first_indexed | 2024-12-22T22:26:47Z |
| format | Article |
| id | doaj.art-615d49f2debe4a0093090f3f047ea73a |
| institution | Directory Open Access Journal |
| issn | 1476-4598 |
| language | English |
| last_indexed | 2024-12-22T22:26:47Z |
| publishDate | 2003-11-01 |
| publisher | BMC |
| record_format | Article |
| series | Molecular Cancer |
| spelling | doaj.art-615d49f2debe4a0093090f3f047ea73a2022-12-21T18:10:31ZengBMCMolecular Cancer1476-45982003-11-01213910.1186/1476-4598-2-39At the crossroads of SUMO and NF-κBSchmidt ChristianKracklauer Martin P<p>Abstract</p> <p>Background</p> <p>Recognition of pathogens by immune receptors leads to activation of macrophages, dendritic cells, and lymphocytes. Signals are communicated to enhance expression of target molecules such as cytokines and adhesion molecules, depending on activation of various inducible transcription factors, among which the family NF-κB transcription factors plays an evolutionarily conserved and critical role. Classical activation of NF-κB involves phosphorylation, polyubiquitination and subsequent degradation of the inhibitor molecules of NF-κB, referred to as IκB. Modification of IκBα, one of the mammalian IκB isoforms, with the small ubiquitin-like modifier (SUMO) results its protection from degradation.</p> <p>Presentation of the hypothesis</p> <p>SUMO-IκBα localizes in the nucleus. The nuclear SUMO-IκBα pool may be dynamic. SUMO-IκBα functions as synergy control factor.</p> <p>Testing the hypothesis</p> <p>Immunoprecipitation from cellular fractions, <sup>35</sup>S methionine pulse-chase, and FRET assays should reveal the localization of SUMO-IκBα and the dynamics of the pool. Expression of SUMOylation defective IκBα in an <it>IκBα </it><sup>-/- </sup>background should yield insights into the function of SUMO-IκBα.</p> <p>Implication of the hypothesis</p> <p>IκBα contains the required SUMOylation motif but IκBβ does not. The suggested study would provide evidence whether or not IκBα and IκBβ can substitute each other. In addition, the suggested assays would reveal a possible redundancy in controlling transcriptional activity of NF-κB.</p>http://www.molecular-cancer.com/content/2/1/39SUMOIκBNF-κBsignaling |
| spellingShingle | Schmidt Christian Kracklauer Martin P At the crossroads of SUMO and NF-κB Molecular Cancer SUMO IκB NF-κB signaling |
| title | At the crossroads of SUMO and NF-κB |
| title_full | At the crossroads of SUMO and NF-κB |
| title_fullStr | At the crossroads of SUMO and NF-κB |
| title_full_unstemmed | At the crossroads of SUMO and NF-κB |
| title_short | At the crossroads of SUMO and NF-κB |
| title_sort | at the crossroads of sumo and nf κb |
| topic | SUMO IκB NF-κB signaling |
| url | http://www.molecular-cancer.com/content/2/1/39 |
| work_keys_str_mv | AT schmidtchristian atthecrossroadsofsumoandnfkb AT kracklauermartinp atthecrossroadsofsumoandnfkb |