SKP1-like-related genes interact with various F-box proteins and may form SCF complexes with Cullin-F-box proteins in wheat.

S-phase kinase-associated protein 1 (SKP1), a core component of the SKP1-Cullin-F-box (SCF) E3 ubiquitin ligase complex, functions as an adaptor protein, connecting cullin and F-box proteins. SKP1 plays crucial roles in cell-cycle progression, transcriptional regulation, flower formation, signal transduction, and many other cellular processes. SKP1-like genes have been largely unstudied in wheat. Here, we isolated six wheat SKP1-like (TaSKP) genes from common wheat (Triticum aestivum) and analyzed the expression patterns of these six genes using reverse transcription-polymerase chain reaction (RT-PCR). Based on gene expression patterns, we divided the genes into two groups. Our data demonstrated that green fluorescent protein-tagged TaSKP proteins were targeted to the plasma membrane or cytoplasm in plant cells. In a yeast two-hybrid system, all TaSKP proteins interacted with TaCFBD, TaSKP1, and TaSKP5, while TaSKP6 interacted with RA and RLK. A BiFC assay suggested that specific combinations of TaSKP and F-box proteins may influence localization patterns in plant cells. TaSKP1, TaSKP5, and TaSKP6 interacted with TaCullin, while TaSKP2, TaSKP3, and TaSKP4 were not found to interact with TaCullin in the yeast two-hybrid system. This evidence indicated that some TaSKP proteins may have the ability to form SCF complexes. Taken together, these data suggested that TaSKP1, TaSKP5, and TaSKP6 proteins may act as a bridge between various F-box proteins and cullin proteins and that TaSKP genes may be involved in various growth and flower development processes.