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

DSpace/Manakin Repository

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

Show simple item record

dc.contributor.author Seibert, Volker
dc.contributor.author Prohl, Corinna
dc.contributor.author Schoultz, Ida
dc.contributor.author Lopez, Rebecca
dc.contributor.author Abderazzaq, Kareem
dc.contributor.author Zhou, Chunshui
dc.contributor.author Wolf, Dieter A
dc.contributor.author Rhee, Edward
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

Files in this item

Files Size Format View
128837.pdf 1.630Mb PDF View/Open

This item appears in the following Collection(s)

Show simple item record

 
 

Search DASH


Advanced Search
 
 

Submitters