SCF ubiquitin ligase complex binding

Definition

Target type: molecularfunction

Binding to a SCF ubiquitin ligase complex. [GOC:dph, GOC:ha, GOC:TermGenie, PMID:19723762]

SCF ubiquitin ligase complexes are multi-protein complexes that play a crucial role in protein degradation through the ubiquitin-proteasome system. They consist of four core components: an F-box protein, a Skp1 protein, a Cul1 protein, and an Rbx1 protein. The F-box protein acts as a substrate recognition subunit, binding to specific target proteins and determining their fate. The Skp1 protein acts as a bridge connecting the F-box protein to the Cul1 protein, which forms a scaffold for the complex. The Rbx1 protein interacts with the E2 ubiquitin-conjugating enzyme, facilitating the transfer of ubiquitin molecules to the target protein.

The molecular function of SCF ubiquitin ligase complex binding involves a series of steps:

1. **Substrate recognition:** The F-box protein within the SCF complex binds to specific recognition motifs on the target protein, often phosphorylation sites or other post-translational modifications. This interaction is highly specific and allows the SCF complex to target only particular proteins for degradation.

2. **Recruitment of the E2 enzyme:** The Rbx1 protein interacts with the E2 ubiquitin-conjugating enzyme, which is responsible for transferring ubiquitin molecules to the target protein. This interaction ensures that the E2 enzyme is properly positioned within the SCF complex for efficient ubiquitination.

3. **Ubiquitination:** The E2 enzyme, guided by the Rbx1 protein, transfers ubiquitin molecules to lysine residues on the target protein. This process is repeated, leading to the formation of a polyubiquitin chain on the target protein.

4. **Proteasomal degradation:** The polyubiquitin chain serves as a signal for the proteasome, a large protein complex responsible for protein degradation. The proteasome recognizes and degrades the ubiquitinated target protein, effectively removing it from the cell.

Therefore, the molecular function of SCF ubiquitin ligase complex binding is to specifically recognize, recruit, and ubiquitinate target proteins, ultimately leading to their degradation by the proteasome. This process plays a critical role in regulating a wide range of cellular processes, including cell cycle control, signal transduction, and DNA damage repair.'
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Proteins (2)

Compounds (10)