COF1 cofilin [Saccharomyces cerevisiae S288C] - Gene

Summary

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Gene symbol: COF1
Gene description: cofilin
Primary source: SGD:S000003973
Locus tag: YLL050C
See related: AllianceGenome:SGD:S000003973
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables actin filament binding activity. Involved in several processes, including Golgi to plasma membrane protein transport; actin filament depolymerization; and actin filament severing. Located in actin cortical patch. Human ortholog(s) of this gene implicated in nemaline myopathy 7. Orthologous to several human genes including CFL2 (cofilin 2) and DSTN (destrin, actin depolymerizing factor). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:: chromosome: XII

Exon count:: 2

Sequence:: Chromosome: XII; NC_001144.5 (39804..40414, complement)

Chromosome XII - NC_001144.5 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001144.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Cyclase-associated protein (CAP) and Cofilin synergize to processively depolymerize actin filament pointed ends at a rate 330-fold faster than spontaneous depolymerization. Single molecule imaging further reveals that hexameric CAP molecules interact with the pointed ends of Cofilin-decorated filaments for several seconds at a time, removing approximately 100 actin subunits per binding event.
Title: Synergy between Cyclase-associated protein and Cofilin accelerates actin filament depolymerization by two orders of magnitude.
Report structural basis for noncanonical substrate recognition of cofilin-1/LIMK1 to regulation actin cytoskeleton dynamics.
Title: Structural Basis for Noncanonical Substrate Recognition of Cofilin/ADF Proteins by LIM Kinases.
Using multi-color total internal reflection fluorescence microscopy, the study shows that Crn1 enhances Cof1-mediated severing by accelerating Cof1 binding to actin filament sides.
Title: Coronin Enhances Actin Filament Severing by Recruiting Cofilin to Filament Sides and Altering F-Actin Conformation.
Data indicate that the combined activities of cofilin and Srv2/CAP lead to enhanced filament severing and support an emerging view that actin disassembly is controlled not by cofilin alone, but by a more complex set of factors working in concert.
Title: Srv2/cyclase-associated protein forms hexameric shurikens that directly catalyze actin filament severing by cofilin.
Findings highlight the conserved role of cofilin and SPCA1/Pmr1 in sorting of the soluble secretory proteins at the trans-Golgi network/late Golgi membranes in eukaryotes.
Title: Cofilin-mediated sorting and export of specific cargo from the Golgi apparatus in yeast.
Cofilin tunes the nucleotide state of actin filaments and severs at bare and decorated segment boundaries.
Title: Cofilin tunes the nucleotide state of actin filaments and severs at bare and decorated segment boundaries.
Data suggest a revised model for the mechanism by which Srv2 promotes actin turnover, in which coordinated activities of its N- and C-terminal halves catalyze sequential steps in recycling cofilin and actin monomers.
Title: Reconstitution and dissection of the 600-kDa Srv2/CAP complex: roles for oligomerization and cofilin-actin binding in driving actin turnover.
Results show that yeast cofilin 1 can efficiently depolymerize and sever yeast actin filaments decorated with either tropomyosin (Tpm)1 or mouse tropomyosins TM1 and TM4.
Title: Intrinsic capability of budding yeast cofilin to promote turnover of tropomyosin-bound actin filaments.
confirms the important role of the N-terminal segment of cofilin in interactions with G-actin
Title: Mapping the cofilin binding site on yeast G-actin by chemical cross-linking.
These results suggest that cofilin-mediated actin filament flux is required for the multiple steps of endocytic trafficking.
Title: Cofilin recruitment and function during actin-mediated endocytosis dictated by actin nucleotide state.

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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 binding	IEA Inferred from Electronic Annotation more info
enables actin filament binding	IBA Inferred from Biological aspect of Ancestor more info
enables actin filament binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in Golgi to plasma membrane protein transport	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in actin filament depolymerization	IBA Inferred from Biological aspect of Ancestor more info
involved_in actin filament depolymerization	IDA Inferred from Direct Assay more info	PubMed
involved_in actin filament depolymerization	IEA Inferred from Electronic Annotation more info
involved_in actin filament organization	IDA Inferred from Direct Assay more info	PubMed
involved_in actin filament organization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in actin filament severing	IBA Inferred from Biological aspect of Ancestor more info
involved_in actin filament severing	IDA Inferred from Direct Assay more info	PubMed
involved_in endocytosis	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in actin cortical patch	IBA Inferred from Biological aspect of Ancestor more info
located_in actin cortical patch	IDA Inferred from Direct Assay more info	PubMed
is_active_in actin cytoskeleton	IBA Inferred from Biological aspect of Ancestor more info
located_in 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
located_in cytoskeleton	IEA Inferred from Electronic Annotation more info
located_in nuclear matrix	IEA Inferred from Electronic Annotation more info
located_in nucleus	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	HDA more info	PubMed

General protein information

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Preferred Names: cofilin

NP_013050.1

Cofilin, involved in pH-dependent actin filament depolarization; binds both actin monomers and filaments and severs filaments; involved in the selective sorting, export of the secretory cargo from the late golgi; genetically interacts with pmr1; thought to be regulated by phosphorylation at SER4; ubiquitous and essential in eukaryotes

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_001144.5 Reference assembly

Range

39804..40414 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001181870.1 → NP_013050.1 TPA: cofilin [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_013050.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VXV8, Q03048, Q05307, Q2XN65

UniProtKB/TrEMBL

A7A0L0, C7GNE5, C8ZCS5, G2WIE9, N1NZH6

Conserved Domains (1) summary

cd11286
Location:4 → 136

ADF_cofilin_like; Cofilin, Destrin, and related actin depolymerizing factors