HOF1 formin-binding protein HOF1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: HOF1
Official Full Name: formin-binding protein HOF1
Primary source: SGD:S000004635
Locus tag: YMR032W
See related: AllianceGenome:SGD:S000004635; FungiDB:YMR032W; VEuPathDB:YMR032W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: CYK2
Summary: Enables actin filament binding activity; myosin II heavy chain binding activity; and phospholipid binding activity. Involved in several processes, including actin filament bundle assembly; cytokinetic process; and negative regulation of supramolecular fiber organization. Located in cellular bud neck contractile ring and cellular bud neck septin ring. Part of HICS complex and MIH complex. Human ortholog(s) of this gene implicated in PAPA syndrome. Orthologous to several human genes including GAS7 (growth arrest specific 7). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See HOF1 in Genome Data Viewer

Location:: chromosome: XIII

Exon count:: 1

Sequence:: Chromosome: XIII; NC_001145.3 (335298..337307)

Chromosome XIII - NC_001145.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001145.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Phosphorylation of the F-BAR protein Hof1 drives septin ring splitting in budding yeast.
Title: Phosphorylation of the F-BAR protein Hof1 drives septin ring splitting in budding yeast.
A septin-Hof1 scaffold at the yeast bud neck binds and organizes actin cables.
Title: A septin-Hof1 scaffold at the yeast bud neck binds and organizes actin cables.
Hof1 and Cyk3 interact directly at the time of cytokinesis by means of their respective SH3 and proline-rich domains
Title: Role of the Hof1-Cyk3 interaction in cleavage-furrow ingression and primary-septum formation during yeast cytokinesis.
Hof1 binds to the Sel1-like repeats (SLRs) of Chs4 via its F-BAR domain and inhibits Chs3-mediated chitin synthesis during cytokinesis. In addition, Hof1 is required for rapid accumulation as well as efficient removal of Chs4 at the division site.
Title: Hof1 and Chs4 Interact via F-BAR Domain and Sel1-like Repeats to Control Extracellular Matrix Deposition during Cytokinesis.
Hof1 PEST motif phosphorylation site mutants did not have cytokinesis defects, indicating that regulation of Hof1 levels does not control the onset of actomyosin ring contraction.
Title: Mutation of Hof1 PEST motif phosphorylation sites leads to retention of Hof1 at the bud neck and a decrease in the rate of myosin contraction.
Aim44p regulates phosphorylation of Hof1p to promote contractile ring closure during cytokinesis in Saccharomyces cerevisiae.
Title: Aim44p regulates phosphorylation of Hof1p to promote contractile ring closure during cytokinesis in budding yeast.
Hof1 may function in cytokinesis by coupling actomyosin ring constriction to primary septum formation through interactions with Myo1 and Chs2.
Title: Targeting and functional mechanisms of the cytokinesis-related F-BAR protein Hof1 during the cell cycle.
Dbf2 coordinates septin and actomyosin ring functions during cytokinesis through the regulation/control of Hof1.
Title: Dual function of the NDR-kinase Dbf2 in the regulation of the F-BAR protein Hof1 during cytokinesis.
59 of 131 in: PLoS One. 2013;8(2) (dup#16) Hof1 and Rvs167 have redundant roles in actomyosin ring function during cytokinesis
Title: Hof1 and Rvs167 have redundant roles in actomyosin ring function during cytokinesis in budding yeast.
Data show that polo-like kinase Cdc5 first phosphorylates Hof1 to allow subsequent phosphorylation by Dbf2-Mob1.
Title: Phosphorylation-dependent regulation of the F-BAR protein Hof1 during cytokinesis.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables actin filament binding	IDA Inferred from Direct Assay more info	PubMed
enables cytoskeletal protein binding	IDA Inferred from Direct Assay more info	PubMed
enables myosin II heavy chain binding	IPI Inferred from Physical Interaction more info	PubMed
enables phospholipid binding	IBA Inferred from Biological aspect of Ancestor more info
enables phospholipid binding	IDA Inferred from Direct Assay more info	PubMed
enables protein-containing complex binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in actin cytoskeleton organization	IEA Inferred from Electronic Annotation more info
involved_in actin filament bundle assembly	IDA Inferred from Direct Assay more info	PubMed
involved_in cell division	IEA Inferred from Electronic Annotation more info
involved_in cytoskeleton organization	IBA Inferred from Biological aspect of Ancestor more info
involved_in mitotic actomyosin contractile ring assembly	IGI Inferred from Genetic Interaction more info	PubMed
involved_in mitotic actomyosin contractile ring assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mitotic actomyosin contractile ring contraction	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mitotic cytokinesis	IGI Inferred from Genetic Interaction more info	PubMed
involved_in mitotic cytokinesis	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of actin nucleation	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of formin-nucleated actin cable assembly	IGI Inferred from Genetic Interaction more info	PubMed
involved_in negative regulation of formin-nucleated actin cable assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in primary cell septum biogenesis	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein localization to cell division site	IGI Inferred from Genetic Interaction more info	PubMed
involved_in regulation of mitotic actomyosin contractile ring contraction	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of HICS complex	IPI Inferred from Physical Interaction more info	PubMed
part_of MIH complex	IDA Inferred from Direct Assay more info	PubMed
part_of MIH complex	IPI Inferred from Physical Interaction more info	PubMed
located_in cell cortex	IDA Inferred from Direct Assay more info	PubMed
is_active_in cell division site	IBA Inferred from Biological aspect of Ancestor more info
located_in cellular bud neck	IDA Inferred from Direct Assay more info	PubMed
located_in cellular bud neck	IEA Inferred from Electronic Annotation more info
located_in cellular bud neck contractile ring	IDA Inferred from Direct Assay more info	PubMed
located_in cellular bud neck septin ring	IDA Inferred from Direct Assay more info	PubMed
located_in cortical actin cytoskeleton	IEA Inferred from Electronic Annotation more info
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytoplasmic side of plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoskeleton	IEA Inferred from Electronic Annotation more info
is_active_in mitotic actomyosin contractile ring, proximal layer	IBA Inferred from Biological aspect of Ancestor more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in site of polarized growth	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: formin-binding protein HOF1

NP_013746.1

F-BAR protein that regulates actin cytoskeleton organization; binds and bundles actin filaments, linking them to septins; required for cytokinesis, actin cable organization, and secretory vesicle trafficking; regulates actomyosin ring dynamics and septin localization; N-term. half controls cell size and actin cable levels, while the C-term. half controls actin cable organization, inhibiting Bnr1p-mediated actin nucleation; forms axial striations/pillars at the bud neck; phosphorylated by Dbf2p

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001145.3 Reference assembly

Range

335298..337307

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182529.1 → NP_013746.1 TPA: formin-binding protein HOF1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_013746.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VZK6, Q05080

UniProtKB/TrEMBL

B3LLT0, C8ZEN9, N1NY76

Conserved Domains (3) summary

smart00055
Location:8 → 92

FCH; Fes/CIP4 homology domain

smart00326
Location:600 → 663

SH3; Src homology 3 domains

TIGR02168
Location:110 → 233

SMC_prok_B; chromosome segregation protein SMC, common bacterial type