F-actin-capping protein subunit alpha; 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 (By similarity).

Probable 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 (By similarity).

Probable 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 (By similarity).

F-actin-capping protein subunit alpha; 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 (By similarity).

Probable 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 (By similarity).

Profilin-1; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization. Coordinates the stochastic dynamic properties of actin filaments by modulating formin- mediated actin nucleation and assembly during axial cell expansion. Binds G-actin and poly-L-proline in vitro. Inhib [...]

Probable 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 (By similarity).

Profilin-2; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Binds G- actin and poly-L-proline with low affinity in vitro. Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization. May be involved in the cross-talk between vesicular trafficking and the actin cytoskeleton. At high concentrations, profilin prevents the pol [...]

Probable 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 (By similarity).

Profilin-3; Binds to actin monomers and regulates the organization of the actin cytoskeleton. Can increase the critical concentration (Cc) of actin assembly in vitro. Acts as downstream effector of the hydrogen sulfide signaling to regulate the assembly and depolymerization of F-actin. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (Probable). Binding to the poly-proline motif of formin induces oligomerization of PRF3. PRF3 oligomers inhibit formin-mediated actin assembly to modulate plant immunity triggered by pathog [...]

Probable 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 (By similarity).

Profilin-4; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Acts redundantly with PRF5 to regulate apical actin polymerization at the tip of pollen tube and control polarized pollen tube growth. Functions probably by favoring formin-mediated actin polymerization at pollen tube tips.

Probable 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 (By similarity).

Profilin-5; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Acts redundantly with PRF4 to regulate apical actin polymerization at the tip of pollen tube and control polarized pollen tube growth. Functions probably by favoring formin-mediated actin polymerization at pollen tube tips.

Formin-like protein 1; Might be involved in the organization and polarity of the actin cytoskeleton. Involved in polar pollen cell growth process by maintaining tip-focused cell membrane expansion for the polar extension of pollen tubes; Belongs to the formin-like family. Class-I subfamily.

Profilin-1; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization. Coordinates the stochastic dynamic properties of actin filaments by modulating formin- mediated actin nucleation and assembly during axial cell expansion. Binds G-actin and poly-L-proline in vitro. Inhib [...]

Formin-like protein 1; Might be involved in the organization and polarity of the actin cytoskeleton. Involved in polar pollen cell growth process by maintaining tip-focused cell membrane expansion for the polar extension of pollen tubes; Belongs to the formin-like family. Class-I subfamily.

Profilin-2; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Binds G- actin and poly-L-proline with low affinity in vitro. Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization. May be involved in the cross-talk between vesicular trafficking and the actin cytoskeleton. At high concentrations, profilin prevents the pol [...]

Formin-like protein 1; Might be involved in the organization and polarity of the actin cytoskeleton. Involved in polar pollen cell growth process by maintaining tip-focused cell membrane expansion for the polar extension of pollen tubes; Belongs to the formin-like family. Class-I subfamily.

Profilin-3; Binds to actin monomers and regulates the organization of the actin cytoskeleton. Can increase the critical concentration (Cc) of actin assembly in vitro. Acts as downstream effector of the hydrogen sulfide signaling to regulate the assembly and depolymerization of F-actin. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (Probable). Binding to the poly-proline motif of formin induces oligomerization of PRF3. PRF3 oligomers inhibit formin-mediated actin assembly to modulate plant immunity triggered by pathog [...]

Formin-like protein 1; Might be involved in the organization and polarity of the actin cytoskeleton. Involved in polar pollen cell growth process by maintaining tip-focused cell membrane expansion for the polar extension of pollen tubes; Belongs to the formin-like family. Class-I subfamily.

Profilin-4; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Acts redundantly with PRF5 to regulate apical actin polymerization at the tip of pollen tube and control polarized pollen tube growth. Functions probably by favoring formin-mediated actin polymerization at pollen tube tips.

Formin-like protein 1; Might be involved in the organization and polarity of the actin cytoskeleton. Involved in polar pollen cell growth process by maintaining tip-focused cell membrane expansion for the polar extension of pollen tubes; Belongs to the formin-like family. Class-I subfamily.

Profilin-5; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Acts redundantly with PRF4 to regulate apical actin polymerization at the tip of pollen tube and control polarized pollen tube growth. Functions probably by favoring formin-mediated actin polymerization at pollen tube tips.

Formin-like protein 19; Belongs to the formin-like family. Class-II subfamily.

Profilin-1; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization. Coordinates the stochastic dynamic properties of actin filaments by modulating formin- mediated actin nucleation and assembly during axial cell expansion. Binds G-actin and poly-L-proline in vitro. Inhib [...]

Formin-like protein 19; Belongs to the formin-like family. Class-II subfamily.

Profilin-2; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Binds G- actin and poly-L-proline with low affinity in vitro. Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization. May be involved in the cross-talk between vesicular trafficking and the actin cytoskeleton. At high concentrations, profilin prevents the pol [...]

Formin-like protein 19; Belongs to the formin-like family. Class-II subfamily.

Profilin-3; Binds to actin monomers and regulates the organization of the actin cytoskeleton. Can increase the critical concentration (Cc) of actin assembly in vitro. Acts as downstream effector of the hydrogen sulfide signaling to regulate the assembly and depolymerization of F-actin. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (Probable). Binding to the poly-proline motif of formin induces oligomerization of PRF3. PRF3 oligomers inhibit formin-mediated actin assembly to modulate plant immunity triggered by pathog [...]

Formin-like protein 19; Belongs to the formin-like family. Class-II subfamily.

Profilin-4; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Acts redundantly with PRF5 to regulate apical actin polymerization at the tip of pollen tube and control polarized pollen tube growth. Functions probably by favoring formin-mediated actin polymerization at pollen tube tips.

Formin-like protein 19; Belongs to the formin-like family. Class-II subfamily.

Profilin-5; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Acts redundantly with PRF4 to regulate apical actin polymerization at the tip of pollen tube and control polarized pollen tube growth. Functions probably by favoring formin-mediated actin polymerization at pollen tube tips.

Formin-like protein 2; Might be involved in the organization and polarity of the actin cytoskeleton; Belongs to the formin-like family. Class-I subfamily.

Profilin-1; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization. Coordinates the stochastic dynamic properties of actin filaments by modulating formin- mediated actin nucleation and assembly during axial cell expansion. Binds G-actin and poly-L-proline in vitro. Inhib [...]

Formin-like protein 2; Might be involved in the organization and polarity of the actin cytoskeleton; Belongs to the formin-like family. Class-I subfamily.

Profilin-2; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Binds G- actin and poly-L-proline with low affinity in vitro. Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization. May be involved in the cross-talk between vesicular trafficking and the actin cytoskeleton. At high concentrations, profilin prevents the pol [...]

Formin-like protein 2; Might be involved in the organization and polarity of the actin cytoskeleton; Belongs to the formin-like family. Class-I subfamily.

Profilin-3; Binds to actin monomers and regulates the organization of the actin cytoskeleton. Can increase the critical concentration (Cc) of actin assembly in vitro. Acts as downstream effector of the hydrogen sulfide signaling to regulate the assembly and depolymerization of F-actin. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (Probable). Binding to the poly-proline motif of formin induces oligomerization of PRF3. PRF3 oligomers inhibit formin-mediated actin assembly to modulate plant immunity triggered by pathog [...]