Combinatorial Diversity of Fission Yeast SCF Ubiquitin Ligases by Homo- and Heterooligomeric Assemblies of the F-Box Proteins Pop1p and Pop2p

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Combinatorial Diversity of Fission Yeast SCF Ubiquitin Ligases by Homo- and Heterooligomeric Assemblies of the F-Box Proteins Pop1p and Pop2p

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Title: Combinatorial Diversity of Fission Yeast SCF Ubiquitin Ligases by Homo- and Heterooligomeric Assemblies of the F-Box Proteins Pop1p and Pop2p
Author: Seibert, Volker; Prohl, Corinna; Schoultz, Ida; Lopez, Rebecca; Abderazzaq, Kareem; Zhou, Chunshui; Wolf, Dieter A; Rhee, Edward

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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.
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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.
Published Version: doi: 10.1186/1471-2091-3-22
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC128837/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:4727712

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