Mechanisms of the innate immune response have been highly conserved throughout evolution. These pathways rely on NF-kB transcription factors to activate the expression of antimicrobial peptides in response to infection. In Drosophila, expression of antibacterial peptides is mediated by endoproteolytic cleavage of Relish, a Drosophila AF-KB homolog. Relish cleavage requires the Drosophila inhibitor-kB kinase complex (dmIKK), which may directly phosphorylate Relish. DmlKK interacts directly with Relish, but this interaction has not been fully characterized. Here, the domains of Relish required for interaction with DmlKK and phosphorylation by DmlKK have been shown via yeast two-hybrid and in-vitro kinase assays.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Love, Ian Michael

Publisher

• Worcester Polytechnic Institute

Identifier

• 04D277M

Advisor

• Adams, David S.

Year

• 2004

Sponsor

• Umass Med Center

Date created

• 2004-01-01

Resource type

• Major Qualifying Project

Major

• Biology & Biotechnology

Rights statement

• In Copyright

License

• All rights reserved