Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homolog of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa).

Phosphatidate phosphatase, converts phosphatidate to diacylglycerol; App1p, Pah1p, Dpp1p, and Lpp1p are responsible for all the phosphatidate phosphatase activity; component of cortical actin patches; interacts with components of endocytic pathway.

Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homolog of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa).

Myosin tail region-interacting protein MTI1; Protein possibly involved in assembly of actin patches; interacts with an actin assembly factor Las17p and with the SH3 domains of Type I myosins Myo3p and Myo5p; localized predominantly to cortical actin patches.

Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homolog of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa).

Protein BSP1; Adapter that links synaptojanins to the cortical actin cytoskeleton; the synaptojanins are Inp52p and Inp53p.

Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homolog of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa).

SH3 domain protein implicated in regulating actin polymerization; able to recruit actin polymerization machinery through its SH3 domains; colocalizes with cortical actin patches and Las17p; interacts with type I myosins.

Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homolog of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa).

Proline-rich protein LAS17; Actin assembly factor; C-terminal WCA domain activates Arp2/3 complex-mediated nucleation of branched actin filaments, polyproline domain nucleates actin filaments independent of Arp2/3; mutants are defective in endocytosis, bud site selection, cytokinesis; human homolog WAS (Wiskott-Aldrich Syndrome) implicated in severe immunodeficiency; human WAS complements yeast null mutant, but only in presence of WIPF1, which mediates localization of WAS to cortical patches.

Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homolog of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa).

LAS seventeen-binding protein 1; Negative regulator of actin nucleation-promoting factor activity; interacts with Las17p, a homolog of human Wiskott-Aldrich Syndrome protein (WASP), via an N-terminal SH3 domain, and along with PIN3 cooperatively inhibits the nucleation of actin filaments; overexpression blocks receptor-mediated endocytosis; protein increases in abundance and forms nuclear foci in response to DNA replication stress; LSB1 has a paralog, PIN3, that arose from the whole genome duplication.

Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homolog of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa).

Protein containing a C-terminal SH3 domain; binds Las17p, which is a homolog of human Wiskott-Aldrich Syndrome protein involved in actin patch assembly and actin polymerization; protein abundance increases in response to DNA replication stress; LSB3 has a paralog, YSC84, that arose from the whole genome duplication.

Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homolog of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa).

Myosin-3; One of two type I myosins; localizes to actin cortical patches; deletion of MYO3 has little effect on growth, but myo3 myo5 double deletion causes severe defects in growth and actin cytoskeleton organization; MYO3 has a paralog, MYO5, that arose from the whole genome duplication; Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.

Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homolog of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa).

[PSI+] inducibility protein 3; Negative regulator of actin nucleation-promoting factor activity; interacts with Las17p, a homolog of human Wiskott-Aldrich Syndrome protein (WASP), via an N-terminal SH3 domain, and along with LSB1 cooperatively inhibits the nucleation of actin filaments; short-lived protein whose levels increase in response to thermal stress; induces the formation of the [PIN+] and [RNQ+] prions when overproduced; PIN3 has a paralog, LSB1, that arose from the whole genome duplication.

Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homolog of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa).

Reduced viability upon starvation protein 167; Calmodulin-binding actin-associated protein; roles in endocytic membrane tabulation and constriction, and exocytosis; N-BAR domain protein that interacts with Rvs161p to regulate actin cytoskeleton, endocytosis, and viability following starvation or osmotic stress; recruited to bud tips by Gyl1p and Gyp5p during polarized growth; homolog of mammalian amphiphysin.

Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homolog of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa).

Actin cytoskeleton-regulatory complex protein SLA1; Cytoskeletal protein binding protein; required for assembly of the cortical actin cytoskeleton; interacts with proteins regulating actin dynamics and proteins required for endocytosis; found in the nucleus and cell cortex; has 3 SH3 domains; Belongs to the SLA1 family.

Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homolog of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa).

Verprolin, proline-rich actin-associated protein; involved in cytoskeletal organization and cytokinesis; promotes actin nucleation and endocytosis; related to mammalian Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP); Belongs to the verprolin family.

Phosphatidate phosphatase, converts phosphatidate to diacylglycerol; App1p, Pah1p, Dpp1p, and Lpp1p are responsible for all the phosphatidate phosphatase activity; component of cortical actin patches; interacts with components of endocytic pathway.

Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homolog of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa).

Phosphatidate phosphatase, converts phosphatidate to diacylglycerol; App1p, Pah1p, Dpp1p, and Lpp1p are responsible for all the phosphatidate phosphatase activity; component of cortical actin patches; interacts with components of endocytic pathway.

Myosin tail region-interacting protein MTI1; Protein possibly involved in assembly of actin patches; interacts with an actin assembly factor Las17p and with the SH3 domains of Type I myosins Myo3p and Myo5p; localized predominantly to cortical actin patches.

Phosphatidate phosphatase, converts phosphatidate to diacylglycerol; App1p, Pah1p, Dpp1p, and Lpp1p are responsible for all the phosphatidate phosphatase activity; component of cortical actin patches; interacts with components of endocytic pathway.

Protein BSP1; Adapter that links synaptojanins to the cortical actin cytoskeleton; the synaptojanins are Inp52p and Inp53p.

Phosphatidate phosphatase, converts phosphatidate to diacylglycerol; App1p, Pah1p, Dpp1p, and Lpp1p are responsible for all the phosphatidate phosphatase activity; component of cortical actin patches; interacts with components of endocytic pathway.

SH3 domain protein implicated in regulating actin polymerization; able to recruit actin polymerization machinery through its SH3 domains; colocalizes with cortical actin patches and Las17p; interacts with type I myosins.

Phosphatidate phosphatase, converts phosphatidate to diacylglycerol; App1p, Pah1p, Dpp1p, and Lpp1p are responsible for all the phosphatidate phosphatase activity; component of cortical actin patches; interacts with components of endocytic pathway.

Proline-rich protein LAS17; Actin assembly factor; C-terminal WCA domain activates Arp2/3 complex-mediated nucleation of branched actin filaments, polyproline domain nucleates actin filaments independent of Arp2/3; mutants are defective in endocytosis, bud site selection, cytokinesis; human homolog WAS (Wiskott-Aldrich Syndrome) implicated in severe immunodeficiency; human WAS complements yeast null mutant, but only in presence of WIPF1, which mediates localization of WAS to cortical patches.

Phosphatidate phosphatase, converts phosphatidate to diacylglycerol; App1p, Pah1p, Dpp1p, and Lpp1p are responsible for all the phosphatidate phosphatase activity; component of cortical actin patches; interacts with components of endocytic pathway.

LAS seventeen-binding protein 1; Negative regulator of actin nucleation-promoting factor activity; interacts with Las17p, a homolog of human Wiskott-Aldrich Syndrome protein (WASP), via an N-terminal SH3 domain, and along with PIN3 cooperatively inhibits the nucleation of actin filaments; overexpression blocks receptor-mediated endocytosis; protein increases in abundance and forms nuclear foci in response to DNA replication stress; LSB1 has a paralog, PIN3, that arose from the whole genome duplication.

Phosphatidate phosphatase, converts phosphatidate to diacylglycerol; App1p, Pah1p, Dpp1p, and Lpp1p are responsible for all the phosphatidate phosphatase activity; component of cortical actin patches; interacts with components of endocytic pathway.

Protein containing a C-terminal SH3 domain; binds Las17p, which is a homolog of human Wiskott-Aldrich Syndrome protein involved in actin patch assembly and actin polymerization; protein abundance increases in response to DNA replication stress; LSB3 has a paralog, YSC84, that arose from the whole genome duplication.

Phosphatidate phosphatase, converts phosphatidate to diacylglycerol; App1p, Pah1p, Dpp1p, and Lpp1p are responsible for all the phosphatidate phosphatase activity; component of cortical actin patches; interacts with components of endocytic pathway.

Myosin-3; One of two type I myosins; localizes to actin cortical patches; deletion of MYO3 has little effect on growth, but myo3 myo5 double deletion causes severe defects in growth and actin cytoskeleton organization; MYO3 has a paralog, MYO5, that arose from the whole genome duplication; Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.