Identification of a conserved F-box protein 6 interactor essential for endocytosis cytokinesis in fission yeast
Résumé
The F-box domain is a degenerated motif consisting of ~40 amino acid residues that specifically bind Skp1, a core component of the SCF (Skp1-Cdc53/Cullin 1-F-box protein) ubiquitin ligase. Recent work, mainly performed in budding yeast, indicates that certain F-box proteins form non-SCF complexes together with Skp1 in the absence of cullins and play various roles in cell cycle and signalling pathways. However it is not established whether these non-SCF complexes are unique to budding yeast or common in other eukaryotes. Here using TAP purification coupled to MudPIT analysis (Multidimensional Protein Identification Technology), we have identified a novel conserved protein, Sip1 in fission yeast, as an interacting partner of an essential F-box protein Pof6. Sip1 is a large HEAT-repeats containing protein (217 kDa) and forms a complex with Pof6 and Skp1. This complex does not contain cullins, indicating that it is a novel non-SCF complex. Like Pof6 and Skp1, Sip1 is essential for cell viability and temperature sensitive sip1 mutants display cell division arrest as binucleate cells with septa. Sip1 localises to the nucleus and dynamic cytoplasmic dots, which turn out to be endocytic vesicles. Consistent with this, sip1 mutants are defective in endocytosis. Furthermore towards the end of cytokinesis, constriction of the actomyosin ring and dissociation of type II myosin and septum materials are substantially delayed in the absence of functional Sip1. These results indicate that the conserved Sip1 protein comprises a novel non-SCF F-box complex that plays an essential role in endocytosis, cytokinesis and cell division.
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