dc.contributor.author | Seibert, Volker | |
dc.contributor.author | Prohl, Corinna | |
dc.contributor.author | Schoultz, Ida | |
dc.contributor.author | Rhee, Edward | |
dc.contributor.author | Lopez, Rebecca | |
dc.contributor.author | Abderazzaq, Kareem | |
dc.contributor.author | Zhou, Chunshui | |
dc.contributor.author | Wolf, Dieter A | |
dc.date.accessioned | 2011-02-18T17:36:46Z | |
dc.date.issued | 2002 | |
dc.identifier.citation | Seibert, Volker, Corinna Prohl, Ida Schoultz, Edward Rhee, Rebecca Lopez, Kareem Abderazzaq, Chunshui Zhou, and Dieter A. Wolf. 2002. Combinatorial diversity of fission yeast SCF ubiquitin ligases by homo- and heterooligomeric assemblies of the F-box proteins Pop1p and Pop2p. BMC Biochemistry 3: 22. | en_US |
dc.identifier.issn | 1471-2091 | en_US |
dc.identifier.uri | http://nrs.harvard.edu/urn-3:HUL.InstRepos:4727712 | |
dc.description.abstract | Background: SCF ubiquitin ligases share the core subunits cullin 1, SKP1, and HRT1/RBX1/ROC1, which associate with different F-box proteins. F-box proteins bind substrates following their phosphorylation upon stimulation of various signaling pathways. Ubiquitin-mediated destruction of the fission yeast cyclin-dependent kinase inhibitor Rum1p depends on two heterooligomerizing F-box proteins, Pop1p and Pop2p. Both proteins interact with the cullin Pcu1p when overexpressed, but it is unknown whether this reflects their co-assembly into bona fide SCF complexes. Results: We have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p. Only the F-box of Pop1p is required for SCFPop1p-Pop2p function, while Pop2p seems to be attracted into the complex through binding to Pop1p. Since all SCFPop1p-Pop2p subunits, except for Pop1p, which is exclusively nuclear, localize to both the nucleus and the cytoplasm, the F-box of Pop2p may be critical for the assembly of cytoplasmic SCFPop2p complexes. In support of this notion, we demonstrate individual SCFPop1p and SCFPop2p complexes bearing ubiquitin ligase activity. Conclusion: Our data suggest that distinct homo- and heterooligomeric assemblies of Pop1p and Pop2p generate combinatorial diversity of SCFPop function in fission yeast. Whereas a heterooligomeric SCFPop1p-Pop2p complex mediates polyubiquitylation of Rum1p, homooligomeric SCFPop1p and SCFPop2p complexes may target unknown nuclear and cytoplasmic substrates. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | BioMed Central | en_US |
dc.relation.isversionof | doi: 10.1186/1471-2091-3-22 | en_US |
dc.relation.hasversion | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC128837/pdf/ | en_US |
dash.license | LAA | |
dc.title | Combinatorial Diversity of Fission Yeast SCF Ubiquitin Ligases by Homo- and Heterooligomeric Assemblies of the F-Box Proteins Pop1p and Pop2p | en_US |
dc.type | Journal Article | en_US |
dc.description.version | Version of Record | en_US |
dc.relation.journal | BMC Biochemistry | en_US |
dash.depositing.author | Rhee, Edward | |
dc.date.available | 2011-02-18T17:36:46Z | |
dash.affiliation.other | HMS^Anaesthesia-Massachusetts General Hospital | en_US |
dc.identifier.doi | 10.1186/1471-2091-3-22 | * |
dash.contributor.affiliated | Rhee, Edward | |