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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
Department of Cancer Cell Biology, Harvard School of Public Health, Boston, USA .
Department of Cancer Cell Biology, Harvard School of Public Health, Boston, USA .
Department of Cancer Cell Biology, Harvard School of Public Health, Boston, USA .ORCID iD: 0000-0002-8391-1576
Department of Cancer Cell Biology, Harvard School of Public Health, Boston, USA .
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2002 (English)In: BMC biochemistry, ISSN 1471-2091, Vol. 3, 1-15 p., 22Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
London, United Kingdom: BioMed Central, 2002. Vol. 3, 1-15 p., 22
National Category
Medical and Health Sciences Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:oru:diva-40022DOI: 10.1186/1471-2091-3-22ISI: 000209092600022PubMedID: 12167173Scopus ID: 2-s2.0-34248339595OAI: oai:DiVA.org:oru-40022DiVA: diva2:774704
Available from: 2014-12-28 Created: 2014-12-28 Last updated: 2015-06-29Bibliographically approved

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