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- Title
Association of human CUL-1 and ubiquitin-conjugating enzyme CDC34 with the F-box protein p45<sup>SKP2</sup>: evidence for evolutionary conservation in the subunit composition of the CDC34-SCF pathway.
- Authors
Lisztwan, Joanna; Marti, Alain; Sutterlüty, Hedwig; Gstaiger, Matthias; Wirbelauer, Christiane; Krek, Wilhelm
- Abstract
In normal and transformed cells, the F-box protein p45SKP2 is required for S phase and forms stable complexes with p19SKP1 and cyclin Acyclin-dependent kinase (CDK)2. Here we identify human CUL-1, a member of the cullin family, and the ubiquitinconjugating enzyme CDC34 as additional partners of p45SKP2 in vivo. CUL-1 also associates with cyclin A and p19SKP1 in vivo and, with p45SKP2, they assemble into a large multiprotein complex. In Saccharomyces cerevisiae, a complex of similar molecular composition (an F-box protein, a member of the cullin family and a homolog of p19SKP1) forms a functional E3 ubiquitin protein ligase complex, designated SCFCDC4, that facilitates ubiquitination of a CDK inhibitor by CDC34. The data presented here imply that the p45SKP2CUL-1p19SKP1 complex may be a human representative of an SCF-type E3 ubiquitin protein ligase. We propose that all eukaryotic cells may use a common ubiquitin conjugation apparatus to promote S phase. Finally, we show that multiprotein complex formation involving p45SKP2CUL-1 and p19SKP1 is governed, in part, by periodic, S phase-specific accumulation of the p45SKP2 subunit and by the p45SKP2-bound cyclin ACDK2. The dependency of p45SKP2p19SKP1 complex formation on cyclin ACDK2 may ensure tight coordination of the activities of the cell cycle clock with those of a potential ubiquitin conjugation pathway.
- Publication
EMBO Journal, 1998, Vol 17, Issue 2, p368
- ISSN
0261-4189
- Publication type
Academic Journal
- DOI
10.1093/emboj/17.2.368