Actin-interacting protein 1; Actin cortical patch component; interacts with the actin depolymerizing factor cofilin; inhibits elongation of aged ADP-actin filaments decorated with cofilin to maintain a high level of assembly-competent actin species; required to restrict cofilin localization to cortical patches; putative regulator of cytokinesis; contains WD repeats; protein increases in abundance and relocalizes from cytoplasm to plasma membrane upon DNA replication stress.

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; Belongs to the actin-binding proteins ADF family.

Actin-interacting protein 1; Actin cortical patch component; interacts with the actin depolymerizing factor cofilin; inhibits elongation of aged ADP-actin filaments decorated with cofilin to maintain a high level of assembly-competent actin species; required to restrict cofilin localization to cortical patches; putative regulator of cytokinesis; contains WD repeats; protein increases in abundance and relocalizes from cytoplasm to plasma membrane upon DNA replication stress.

Profilin; binds actin, phosphatidylinositol 4,5-bisphosphate, and polyproline regions; involved in cytoskeleton organization; required for normal timing of actin polymerization in response to thermal stress; protein abundance increases in response to DNA replication stress; highly conserved protein; human PFN1 (profilin 1) complements temperature sensitive pfy1 mutants, PFN1 mutations are a rare cause of ALS.

Actin-interacting protein 1; Actin cortical patch component; interacts with the actin depolymerizing factor cofilin; inhibits elongation of aged ADP-actin filaments decorated with cofilin to maintain a high level of assembly-competent actin species; required to restrict cofilin localization to cortical patches; putative regulator of cytokinesis; contains WD repeats; protein increases in abundance and relocalizes from cytoplasm to plasma membrane upon DNA replication stress.

CAP (cyclase-associated protein); N-terminus binds adenylate cyclase and facilitates activation by RAS; N-terminus forms novel hexameric star-shaped shuriken structures that directly catalyze cofilin-mediated severing of actin filaments; C-terminus binds and recycles cofilin bound, ADP-actin monomers, facilitating regulation of actin dynamics and cell morphogenesis; N- and C-termini can function as physically separate proteins; mCAP1 is the mouse homolog.

Actin-interacting protein 1; Actin cortical patch component; interacts with the actin depolymerizing factor cofilin; inhibits elongation of aged ADP-actin filaments decorated with cofilin to maintain a high level of assembly-competent actin species; required to restrict cofilin localization to cortical patches; putative regulator of cytokinesis; contains WD repeats; protein increases in abundance and relocalizes from cytoplasm to plasma membrane upon DNA replication stress.

Twinfilin-1; Twinfilin; highly conserved actin monomer-sequestering protein involved in regulation of the cortical actin cytoskeleton; coordinates actin filament severing and monomer sequestering at sites of rapid actin turnover; composed of two cofilin-like regions, stimulates actin depolymerization as does the mouse homolog, mTwf1.

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; Belongs to the actin-binding proteins ADF family.

Actin-interacting protein 1; Actin cortical patch component; interacts with the actin depolymerizing factor cofilin; inhibits elongation of aged ADP-actin filaments decorated with cofilin to maintain a high level of assembly-competent actin species; required to restrict cofilin localization to cortical patches; putative regulator of cytokinesis; contains WD repeats; protein increases in abundance and relocalizes from cytoplasm to plasma membrane upon DNA replication stress.

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; Belongs to the actin-binding proteins ADF family.

Profilin; binds actin, phosphatidylinositol 4,5-bisphosphate, and polyproline regions; involved in cytoskeleton organization; required for normal timing of actin polymerization in response to thermal stress; protein abundance increases in response to DNA replication stress; highly conserved protein; human PFN1 (profilin 1) complements temperature sensitive pfy1 mutants, PFN1 mutations are a rare cause of ALS.

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; Belongs to the actin-binding proteins ADF family.

CAP (cyclase-associated protein); N-terminus binds adenylate cyclase and facilitates activation by RAS; N-terminus forms novel hexameric star-shaped shuriken structures that directly catalyze cofilin-mediated severing of actin filaments; C-terminus binds and recycles cofilin bound, ADP-actin monomers, facilitating regulation of actin dynamics and cell morphogenesis; N- and C-termini can function as physically separate proteins; mCAP1 is the mouse homolog.

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; Belongs to the actin-binding proteins ADF family.

Twinfilin-1; Twinfilin; highly conserved actin monomer-sequestering protein involved in regulation of the cortical actin cytoskeleton; coordinates actin filament severing and monomer sequestering at sites of rapid actin turnover; composed of two cofilin-like regions, stimulates actin depolymerization as does the mouse homolog, mTwf1.

Profilin; binds actin, phosphatidylinositol 4,5-bisphosphate, and polyproline regions; involved in cytoskeleton organization; required for normal timing of actin polymerization in response to thermal stress; protein abundance increases in response to DNA replication stress; highly conserved protein; human PFN1 (profilin 1) complements temperature sensitive pfy1 mutants, PFN1 mutations are a rare cause of ALS.

Actin-interacting protein 1; Actin cortical patch component; interacts with the actin depolymerizing factor cofilin; inhibits elongation of aged ADP-actin filaments decorated with cofilin to maintain a high level of assembly-competent actin species; required to restrict cofilin localization to cortical patches; putative regulator of cytokinesis; contains WD repeats; protein increases in abundance and relocalizes from cytoplasm to plasma membrane upon DNA replication stress.

Profilin; binds actin, phosphatidylinositol 4,5-bisphosphate, and polyproline regions; involved in cytoskeleton organization; required for normal timing of actin polymerization in response to thermal stress; protein abundance increases in response to DNA replication stress; highly conserved protein; human PFN1 (profilin 1) complements temperature sensitive pfy1 mutants, PFN1 mutations are a rare cause of ALS.

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; Belongs to the actin-binding proteins ADF family.

Profilin; binds actin, phosphatidylinositol 4,5-bisphosphate, and polyproline regions; involved in cytoskeleton organization; required for normal timing of actin polymerization in response to thermal stress; protein abundance increases in response to DNA replication stress; highly conserved protein; human PFN1 (profilin 1) complements temperature sensitive pfy1 mutants, PFN1 mutations are a rare cause of ALS.

CAP (cyclase-associated protein); N-terminus binds adenylate cyclase and facilitates activation by RAS; N-terminus forms novel hexameric star-shaped shuriken structures that directly catalyze cofilin-mediated severing of actin filaments; C-terminus binds and recycles cofilin bound, ADP-actin monomers, facilitating regulation of actin dynamics and cell morphogenesis; N- and C-termini can function as physically separate proteins; mCAP1 is the mouse homolog.

Profilin; binds actin, phosphatidylinositol 4,5-bisphosphate, and polyproline regions; involved in cytoskeleton organization; required for normal timing of actin polymerization in response to thermal stress; protein abundance increases in response to DNA replication stress; highly conserved protein; human PFN1 (profilin 1) complements temperature sensitive pfy1 mutants, PFN1 mutations are a rare cause of ALS.

Twinfilin-1; Twinfilin; highly conserved actin monomer-sequestering protein involved in regulation of the cortical actin cytoskeleton; coordinates actin filament severing and monomer sequestering at sites of rapid actin turnover; composed of two cofilin-like regions, stimulates actin depolymerization as does the mouse homolog, mTwf1.

CAP (cyclase-associated protein); N-terminus binds adenylate cyclase and facilitates activation by RAS; N-terminus forms novel hexameric star-shaped shuriken structures that directly catalyze cofilin-mediated severing of actin filaments; C-terminus binds and recycles cofilin bound, ADP-actin monomers, facilitating regulation of actin dynamics and cell morphogenesis; N- and C-termini can function as physically separate proteins; mCAP1 is the mouse homolog.

Actin-interacting protein 1; Actin cortical patch component; interacts with the actin depolymerizing factor cofilin; inhibits elongation of aged ADP-actin filaments decorated with cofilin to maintain a high level of assembly-competent actin species; required to restrict cofilin localization to cortical patches; putative regulator of cytokinesis; contains WD repeats; protein increases in abundance and relocalizes from cytoplasm to plasma membrane upon DNA replication stress.

CAP (cyclase-associated protein); N-terminus binds adenylate cyclase and facilitates activation by RAS; N-terminus forms novel hexameric star-shaped shuriken structures that directly catalyze cofilin-mediated severing of actin filaments; C-terminus binds and recycles cofilin bound, ADP-actin monomers, facilitating regulation of actin dynamics and cell morphogenesis; N- and C-termini can function as physically separate proteins; mCAP1 is the mouse homolog.

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; Belongs to the actin-binding proteins ADF family.

CAP (cyclase-associated protein); N-terminus binds adenylate cyclase and facilitates activation by RAS; N-terminus forms novel hexameric star-shaped shuriken structures that directly catalyze cofilin-mediated severing of actin filaments; C-terminus binds and recycles cofilin bound, ADP-actin monomers, facilitating regulation of actin dynamics and cell morphogenesis; N- and C-termini can function as physically separate proteins; mCAP1 is the mouse homolog.

Profilin; binds actin, phosphatidylinositol 4,5-bisphosphate, and polyproline regions; involved in cytoskeleton organization; required for normal timing of actin polymerization in response to thermal stress; protein abundance increases in response to DNA replication stress; highly conserved protein; human PFN1 (profilin 1) complements temperature sensitive pfy1 mutants, PFN1 mutations are a rare cause of ALS.

CAP (cyclase-associated protein); N-terminus binds adenylate cyclase and facilitates activation by RAS; N-terminus forms novel hexameric star-shaped shuriken structures that directly catalyze cofilin-mediated severing of actin filaments; C-terminus binds and recycles cofilin bound, ADP-actin monomers, facilitating regulation of actin dynamics and cell morphogenesis; N- and C-termini can function as physically separate proteins; mCAP1 is the mouse homolog.

Twinfilin-1; Twinfilin; highly conserved actin monomer-sequestering protein involved in regulation of the cortical actin cytoskeleton; coordinates actin filament severing and monomer sequestering at sites of rapid actin turnover; composed of two cofilin-like regions, stimulates actin depolymerization as does the mouse homolog, mTwf1.

Twinfilin-1; Twinfilin; highly conserved actin monomer-sequestering protein involved in regulation of the cortical actin cytoskeleton; coordinates actin filament severing and monomer sequestering at sites of rapid actin turnover; composed of two cofilin-like regions, stimulates actin depolymerization as does the mouse homolog, mTwf1.

Actin-interacting protein 1; Actin cortical patch component; interacts with the actin depolymerizing factor cofilin; inhibits elongation of aged ADP-actin filaments decorated with cofilin to maintain a high level of assembly-competent actin species; required to restrict cofilin localization to cortical patches; putative regulator of cytokinesis; contains WD repeats; protein increases in abundance and relocalizes from cytoplasm to plasma membrane upon DNA replication stress.

Twinfilin-1; Twinfilin; highly conserved actin monomer-sequestering protein involved in regulation of the cortical actin cytoskeleton; coordinates actin filament severing and monomer sequestering at sites of rapid actin turnover; composed of two cofilin-like regions, stimulates actin depolymerization as does the mouse homolog, mTwf1.

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; Belongs to the actin-binding proteins ADF family.

Twinfilin-1; Twinfilin; highly conserved actin monomer-sequestering protein involved in regulation of the cortical actin cytoskeleton; coordinates actin filament severing and monomer sequestering at sites of rapid actin turnover; composed of two cofilin-like regions, stimulates actin depolymerization as does the mouse homolog, mTwf1.

Profilin; binds actin, phosphatidylinositol 4,5-bisphosphate, and polyproline regions; involved in cytoskeleton organization; required for normal timing of actin polymerization in response to thermal stress; protein abundance increases in response to DNA replication stress; highly conserved protein; human PFN1 (profilin 1) complements temperature sensitive pfy1 mutants, PFN1 mutations are a rare cause of ALS.

Twinfilin-1; Twinfilin; highly conserved actin monomer-sequestering protein involved in regulation of the cortical actin cytoskeleton; coordinates actin filament severing and monomer sequestering at sites of rapid actin turnover; composed of two cofilin-like regions, stimulates actin depolymerization as does the mouse homolog, mTwf1.

CAP (cyclase-associated protein); N-terminus binds adenylate cyclase and facilitates activation by RAS; N-terminus forms novel hexameric star-shaped shuriken structures that directly catalyze cofilin-mediated severing of actin filaments; C-terminus binds and recycles cofilin bound, ADP-actin monomers, facilitating regulation of actin dynamics and cell morphogenesis; N- and C-termini can function as physically separate proteins; mCAP1 is the mouse homolog.