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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Authors: | Volker Seibert Corinna Prohl Ida Schoultz Edward Rhee Rebecca Lopez Kareem Abderazzaq Chunshui Zhou Dieter A Wolf |
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Institution: | (1) Department of Cancer Cell Biology, Harvard School of Public Health, Boston, MA, USA |
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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. |
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