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In addition, based on overexpression, distinct SCF Pop1pand SCF Pop2pcomplexes were proposed to target unknown substrates, but no biochemical evidence of their activity was provided [ 18 ] . To address these questions, we cloned two additional subunits of SCF Popand performed a detailed characterization of its activity in vitro and in vivo . Our results indicate that heterooligomeric SCF Pop1p-Pop2pmediates Rum1p ubiquitylation whereas distinct SCF Pop1pand SCF Pop2pcomplexes target unknown nuclear and cytoplasmic substrates, thereby generating combinatorial diversity of SCF function in fission yeast.
Similarly, β-TRCP1 and 2, which target IκBα for degradation as homooligomers, form heterooligomers that each bind SCF core subunits, although no biochemical activity for this heterooligomeric complex was demonstrated [ 29 ] . Finally, Pop1p and Pop2p homooligomerize, at least when overexpressed [ 18 ] , indicating that both F-box proteins may also be present as homooligomers in individual SCF Pop1pand SCF Pop2p, respectively.
Individual SCF Pop1pand SCF Pop2pcomplexes bearing ubiquitin ligase activity
While these data support the existence of distinct SCF Pop1pand SCF Pop2pcomplexes, individual binding of Pop1p and Pop2p to SCF core components in the absence of their heterodimerizing F-box protein partners does not rule out the possibility that these complexes represent inactive intermediates formed during the normal assembly of functional SCF Pop1p-Pop2pcomplexes.
In the wild type lenses, typical cross-sectional patterns of fiber cells organized in radial columns were observed (Figure 3K,3N,3Pand 3S).
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