F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Cofilin; Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with [...]

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Centractin; Core component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding. The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. Arp1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. Required for proper orientation of the mitotic spindle (By similarity).

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Actin-related protein 2; Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity). During cytokinesis it colocalizes to the cortical actin patches until spetation is complete. Has a role in the mobility of these patches. Essential for viability.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Actin-related protein 3; Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity). May be involved in cytokinesis.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Cell division control protein 12; Plays a role in the cell cycle. Involved in cytokinesis. Component of the cell division ring. In the absence of profilin, caps the barbed end of actin filaments, thus preventing subunit addition and dissociation. In the presence of profilin, nucleates actin filaments that grow rapidly from their barbed ends. Belongs to the formin homology family. BNI1 subfamily.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Profilin; Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. In S.pombe, it is essential for cytokinesis.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Myosin regulatory light chain cdc4; Involved in cytokinesis. Required for the formation and function of the contractile ring.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Fimbrin; Binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Plays a role in cytokinesis. Plays important roles in mating and in spore formation.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Protein hob3; Involved in cytokinesis and septation where it has a role in the localization of F-actin.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Myosin-1; Type-I myosin implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Contributes to proper septation by transporting vesicles containing septal material to the division site and is involved in the formation of sterol-rich membrane domains at the cell division site. Required also for mating.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Myosin type-2 heavy chain 1; Required for cell division. It is a component of the cdc12 'spot', a structure thought to mark the site of septation. May work in conjunction with myo3; Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Myosin-52; Involved in cell wall deposition where it has a role in the localization of mok1; Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Myosin type-2 heavy chain 2; Stabilizes the F-actin cables forming the F-actin ring that surrounds the nucleus during interphase. May work in conjunction with myo2; Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

GTP-binding protein rho1; Involved in the regulation of cell wall growth and actin cytoskeleton organization. Activates (1,3)-beta-D-glucan synthase. Belongs to the small GTPase superfamily. Rho family.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Ras GTPase-activating-like protein rng2; Required for cytokinesis. Component of the contractile F- actin ring; required for its construction following assembly of F-actin at the division site.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Microtubule-associated protein ssm4; Binds to nuclear microtubules with the effect of either modifying their structure or function. This then promotes meiotic nuclear division.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Verprolin; Involved in cytoskeletal organization and cellular growth. May exert its effects on the cytoskeleton directly, or indirectly via proline-binding proteins such as profilin or proteins possessing SH3 domains. Plays a role in actin patch assembly by enhancing the ability of myo1 to stimulate actin polymerization by the Arp2/3 complex.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Wiskott-Aldrich syndrome protein homolog 1; Has a role in regulating actin assembly, so regulating polarized growth.

Cofilin; Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with [...]

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.

Cofilin; Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with [...]

Centractin; Core component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding. The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. Arp1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. Required for proper orientation of the mitotic spindle (By similarity).