PLK1
Gene Ontology Biological Process
- G2 DNA damage checkpoint [IDA]
- G2/M transition of mitotic cell cycle [IDA, TAS]
- activation of mitotic anaphase-promoting complex activity [IDA]
- anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [TAS]
- cell proliferation [TAS]
- centrosome organization [IMP]
- cytokinesis [IDA, IMP]
- establishment of protein localization [IMP]
- metaphase/anaphase transition of mitotic cell cycle [TAS]
- microtubule bundle formation [IDA]
- mitotic cell cycle [TAS]
- mitotic cytokinesis [IDA]
- mitotic nuclear division [IDA, IMP]
- mitotic nuclear envelope disassembly [TAS]
- mitotic sister chromatid segregation [IMP]
- mitotic spindle assembly checkpoint [IMP]
- negative regulation of apoptotic process [IMP]
- negative regulation of cyclin-dependent protein serine/threonine kinase activity [IMP]
- negative regulation of transcription from RNA polymerase II promoter [IMP]
- peptidyl-serine phosphorylation [IDA]
- positive regulation of peptidyl-threonine phosphorylation [IMP]
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process [IMP]
- positive regulation of proteolysis [IDA]
- positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- positive regulation of ubiquitin-protein transferase activity [IMP]
- protein destabilization [IDA]
- protein localization to chromatin [IDA]
- protein phosphorylation [IDA]
- protein ubiquitination [IDA]
- regulation of cell cycle [TAS]
- regulation of mitotic cell cycle [IMP]
- regulation of mitotic metaphase/anaphase transition [IMP]
- regulation of protein binding [IMP]
- regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
VIM
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Phosphorylation)
An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.
Publication
Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis.
Several kinases phosphorylate vimentin, the most common intermediate filament protein, in mitosis. Aurora-B and Rho-kinase regulate vimentin filament separation through the cleavage furrow-specific vimentin phosphorylation. Cdk1 also phosphorylates vimentin from prometaphase to metaphase, but its significance has remained unknown. Here we demonstrated a direct interaction between Plk1 and vimentin-Ser55 phosphorylated by Cdk1, an event that led to Plk1 activation and ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| VIM PLK1 | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | 42.5 | BioGRID | 3010590 | |
| PLK1 VIM | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - |
Curated By
- BioGRID