Spider Mite Control in Soybeans, 1998b

Patton, T. W.; Dively, Galen P.

doi:10.1093/amt/24.1.f114

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“…These proteins recognize speci®cally phosphorylated substrates and recruit them to an E3 ubiquitin ligase SCF (Skp1-Cdc53-F-box protein; reviewed in Krek, 1998;Elledge and Harper, 1998;Patton et al, 1998b). A number of yeast substrates (Sic1, Far1, Cln2) are ubiquitinated upon association with Skp1-Cdc53 complex through a variety of F-box proteins (Patton et al, 1998b). The latter interact with Skp1 via the F-box..…”

Section: Introductionmentioning

confidence: 99%

HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IκB and β-catenin

Fuchs

Chen

Xiong³

et al. 1999

Oncogene

164

163

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SCF E3 ubiquitin ligases mediate ubiquitination and proteasome-dependent degradation of phosphorylated substrates. We identi®ed a human F-box/WD40 repeats protein (HOS), which is homologous to Slimb/hbTrCP. Being a part of SCF complex with Skp1 and Cullin1, HOS speci®cally interacted with the phosphorylated IkB and b-catenin, targeting these proteins for proteasomedependent degradation in vivo. This targeting required Cullin1 as expression of a mutant Cullin1 abrogated the degradation of IkB and of b-catenin. Mutant HOS which lacks the F-box blocked TNFa-induced degradation of IkB as well as GSK3b-mediated degradation of b-catenin. This mutant also inhibited NF-kB transactivation and increased the b-catenin-dependent transcription activity of Tcf. These results demonstrate that SCF HOS E3 ubiquitin ligase regulate both NF-kB and b-catenin signaling pathways.

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Section: Introductionmentioning

confidence: 99%