MYO1
Gene Ontology Biological Process
- actin cortical patch assembly [IGI]
- actin cortical patch localization [IMP]
- actin cytoskeleton organization [IMP]
- actin filament organization [IMP]
- actin nucleation [IDA, IGI]
- ascospore wall assembly [IMP]
- endocytosis [ISO]
- establishment or maintenance of cell polarity regulating cell shape [IMP]
- plasma membrane raft distribution [IMP]
- positive regulation of actin nucleation [IMP]
- regulation of endocytosis [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
WSP1
Gene Ontology Biological Process
- G1 to G0 transition [IMP]
- actin cortical patch assembly [IGI]
- actin cortical patch internalization [IMP]
- actin filament polymerization [IMP]
- actin nucleation [IDA, IGI]
- cellular response to nitrogen starvation [IMP]
- endocytosis [IMP]
- establishment or maintenance of cell polarity regulating cell shape [IGI]
- fungal-type cell wall biogenesis [IMP]
- mitotic actomyosin contractile ring assembly [IMP]
- mitotic actomyosin contractile ring contraction [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Affinity Capture-MS
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.
Publication
Membrane binding of endocytic myosin-1s is inhibited by a class of ankyrin repeat proteins.
Myosin-1s are monomeric actin-based motors that function at membranes. Myo1 is the single myosin-1 isoform in Schizosaccharomyces pombe that works redundantly with Wsp1-Vrp1 to activate the Arp2/3 complex for endocytosis. Here, we identified Ank1 as an uncharacterized cytoplasmic Myo1 binding partner. We found that in ank1? cells, Myo1 dramatically redistributed from endocytic patches to decorate the entire plasma membrane and ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| WSP1 MYO1 | Affinity Capture-RNA Affinity Capture-RNA An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and associated RNA species identified by Northern blot, RT-PCR, affinity labeling, sequencing, or microarray analysis. | Low | - | BioGRID | - | |
| MYO1 WSP1 | Affinity Capture-RNA Affinity Capture-RNA An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and associated RNA species identified by Northern blot, RT-PCR, affinity labeling, sequencing, or microarray analysis. | Low | - | BioGRID | - | |
| MYO1 WSP1 | Co-localization Co-localization Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments. | Low | - | BioGRID | - | |
| MYO1 WSP1 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
| MYO1 WSP1 | Synthetic Lethality Synthetic Lethality A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition. | Low | - | BioGRID | 559747 | |
| MYO1 WSP1 | Synthetic Lethality Synthetic Lethality A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition. | Low | - | BioGRID | 247403 | |
| WSP1 MYO1 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - |