|
 |
|
|
|
EMBO reports 1, 4, 347–352 (2000)
doi:10.1093/embo-reports/kvd072
Published online: October 2000
Activation of the Drosophila NF- B factor Relish by rapid endoproteolytic cleavage
Svenja Stöven1, Istvan Ando3, Latha Kadalayil4, Ylva Engström2 & Dan Hultmark1
|
|
|
|
1 Umeå Center for Molecular Pathogenesis, Umeå University, S-901 87 Umeå Sweden
2 Department of Molecular Biology, Stockholm University, S-106 91 Stockholm, Sweden
3 Present address: Institute of Genetics, Biological Research Center of the Hungarian Academy of Sciences, 6701 Szeged, Hungary
4 Present address: Department of Biochemistry, Stockholm University, S-10691 Stockholm, Sweden
To whom correspondence should be addressed
Dan Hultmark Tel: +46 90 7856778; Fax: +46 90 778007; dan.hultmark@ucmp.umu.se
Received 5 May 2000; Accepted 15 August 2000.
|
|
|
|
Abstract
The Rel/NF-B transcription factor Relish plays a key role in the humoral immune response in Drosophila. We now find that activation of this innate immune response is preceded by rapid proteolytic cleavage of Relish into two parts. An N-terminal fragment, containing the DNA-binding Rel homology domain, translocates to the nucleus where it binds to the promoter of the Cecropin A1 gene and probably to the promoters of other antimicrobial peptide genes. The C-terminal IB-like fragment remains in the cytoplasm. This endoproteolytic cleavage does not involve the proteasome, requires the DREDD caspase, and is different from previously described mechanisms for Rel factor activation.
|
|
top  |
|
|
|
