Abstract:
BACKGROUND: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-kappaB transcription factors plays an evolutionarily conserved and critical role. Classical activation of NF-kappaB involves phosphorylation, polyubiquitination and subsequent degradation of the inhibitor molecules of NF-kappaB, referred to as IkappaB. Modification of IkappaBalpha, one of the mammalian IkappaB isoforms, with the small ubiquitin-like modifier (SUMO) results its protection from degradation. PRESENTATION OF THE HYPOTHESIS:SUMO-IkappaBalpha localizes in the nucleus. The nuclear SUMO-IkappaBalpha pool may be dynamic. SUMO-IkappaBalpha functions as synergy control factor. TESTING THE HYPOTHESIS:Immunoprecipitation from cellular fractions, 35S methionine pulse-chase, and FRET assays should reveal the localization of SUMO-IkappaBalpha and the dynamics of the pool. Expression of SUMOylation defective IkappaBalpha in an IkappaBalpha -/- background should yield insights into the function of SUMO-IkappaBalpha. IMPLICATION OF THE HYPOTHESIS:IkappaBalpha contains the required SUMOylation motif but IkappaBbeta does not. The suggested study would provide evidence whether or not IkappaBalpha and IkappaBbeta can substitute each other. In addition, the suggested assays would reveal a possible redundancy in controlling transcriptional activity of NF-kappaB.
journal_name
Mol Cancerjournal_title
Molecular cancerauthors
Kracklauer MP,Schmidt Cdoi
10.1186/1476-4598-2-39keywords:
subject
Has Abstractpub_date
2003-11-05 00:00:00pages
39issn
1476-4598pii
1476-4598-2-39journal_volume
2pub_type
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