BAIT

HOF1

CYK2, formin-binding protein HOF1, L000004406, YMR032W
SH3 domain-containing protein required for cytokinesis; localized to bud neck; phosphorylated by Dbf2p; regulates actomyosin ring dynamics and septin localization; interacts with the formins, Bni1p and Bnr1p, and with Cyk3p, Vrp1p, and Bni5p
GO Process (3)
GO Function (1)
GO Component (3)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

SHS1

SEP7, septin SHS1, YDL225W
Component of the septin ring that is required for cytokinesis; septins are GTP-binding proteins that assemble into rod-like hetero-oligomers that can associate with other rods to form filaments; septin rings at the mother-bud neck act as scaffolds for recruiting cell division factors and as barriers to prevent diffusion of specific proteins; undergoes sumoylation and phosphorylation during mitosis; protein abundance increases in response to DNA replication stress
Saccharomyces cerevisiae (S288c)

Synthetic Growth Defect

A genetic interaction is inferred when mutations in separate genes, each of which alone causes a minimal phenotype, result in a significant growth defect under a given condition when combined in the same cell.

Publication

Phosphorylation of the F-BAR protein Hof1 drives septin ring splitting in budding yeast.

Varela Salgado M, Adriaans IE, Touati SA, Ibanes S, Lai-Kee-Him J, Ancelin A, Cipelletti L, Picas L, Piatti S

A double septin ring accompanies cytokinesis in yeasts and mammalian cells. In budding yeast, reorganisation of the septin collar at the bud neck into a dynamic double ring is essential for actomyosin ring constriction and cytokinesis. Septin reorganisation requires the Mitotic Exit Network (MEN), a kinase cascade essential for cytokinesis. However, the effectors of MEN in this process are unknown. ... [more]

Nat Commun Apr. 22, 2024; 15(1);3383 [Pubmed: 38649354]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: vegetative growth (APO:0000106)

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
SHS1 HOF1
PCA
PCA

A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.

Low-BioGRID
835384
SHS1 HOF1
Phenotypic Enhancement
Phenotypic Enhancement

A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene.

Low-BioGRID
856728
HOF1 SHS1
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
1277533
SHS1 HOF1
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
856722

Curated By

  • BioGRID