| + |
PPP1R9B | up-regulates 
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269179 |
|
|
Mus musculus |
Neuro-2a Cell |
| pmid |
sentence |
| 15996550 |
Neurabin and spinophilin are preferentially expressed in neurons, where they are highly localized to dendritic spines via an interaction with F-actin. The results obtained in the present study suggest a mechanism by which neurabin or spinophilin contributes to the organization of the F-actin cytoskeleton in dendritic spines, and in turn to the regulation of spine morphology, via the activity-dependent recruitment of the Rho-specific GEF Lfc |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
GAS2L3 | up-regulates
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273702 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24706950 |
Previous work has shown that members of the growth-arrest-specific 2 (GAS2) family mediate the crosstalk between filamentous actin (F-actin) and MTs, but the molecular basis of this process remained unclear. By using fluorescence microscopy, we demonstrate that three members of this family, GAS2-like 1, GAS2-like 2 and GAS2-like 3 (G2L1, G2L2 and G2L3, also known as GAS2L1, GAS2L2 and GAS2L3, respectively) are differentially involved in mediating the crosstalk between F-actin and MTs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
F-actin_assembly | up-regulates
|
Dendritic_spine_morphogenesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266597 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14684878 |
Dendritic spines are small protrusions found on dendrites of principal neurons of mammalian brain. Serving as postsynaptic compartments for individual excitatory inputs, spines show rapid movements and shape changes that are influenced by synaptic activity. The structural modifications of spines are believed to represent morphological correlates of synaptic plasticity. The form and motility of spines are determined mainly by the actin cytoskeleton |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ARP2/3 | up-regulates
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251511 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12479800 |
The Arp2/3 complex concentrates at leading edges, where it catalyzes the growth of branched actin networks that are believed to provide the protrusive force for leading edge extension. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | T cell activation |
| + |
PPP1R9A | up-regulates
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269180 |
|
|
Mus musculus |
Neuro-2a Cell |
| pmid |
sentence |
| 15996550 |
Neurabin and spinophilin are preferentially expressed in neurons, where they are highly localized to dendritic spines via an interaction with F-actin. The results obtained in the present study suggest a mechanism by which neurabin or spinophilin contributes to the organization of the F-actin cytoskeleton in dendritic spines, and in turn to the regulation of spine morphology, via the activity-dependent recruitment of the Rho-specific GEF Lfc |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
F-actin_assembly | down-regulates 
|
LATS1 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201522 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23450633 |
Ga12/13 recruitment of rho-gefs causes rhoa activation and f-actin assembly, which promotes lats1/lat2 inactivation by an unknown, but myosin-independent mechanism. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Hippo Signaling |
| + |
F-actin_assembly | up-regulates
|
Platelet_morphogenesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261839 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 27871158 |
Each step in platelet shape change involves the participation of a variety of actin filament-related proteins that are highly concentrated in platelets (Fig. 1). In resting human platelets, the actin filaments from the core to the membrane skeleton are tightly bound to the plasma membrane by GP1b/IX-filamin A complexes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
F-actin_assembly | down-regulates
|
LATS1/2 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269861 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23450633 |
Ga12/13 recruitment of rho-gefs causes rhoa activation and f-actin assembly, which promotes lats1/lat2 inactivation by an unknown, but myosin-independent mechanism. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Hippo Signaling |
| + |
WRC complex | up-regulates
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253578 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20332100 |
The activated WAVE complex at the leading edge of lamellipodia promotes actin polymerization at the plasma membrane by activating the Arp2/3 complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
F-actin_assembly | down-regulates
|
Platelet_degranulation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266000 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 23805129 |
Inhibition of actin polymerization also augments the kinetics and degree of alpha-granule release (Flaumenhaft et al., 2005). These results suggest that F-actin disassembly might actually be required for normal granule secretion and that activation-mediated granule release is related to actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Non-erythrocytic spectrin | up-regulates 
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266031 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24302288 |
Spectrin is a member of the F-actin-crosslinking protein superfamily. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CD2AP | up-regulates quantity
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264769 |
|
|
Homo sapiens |
HEK-293 Cell, U2-OS Cell |
| pmid |
sentence |
| 29175910 |
One such regulator is the adaptor protein CD2AP, which delivers capping proteins to the barbed ends of polymerizing F-actin. Capping growing filaments can promote the formation of actin branches by increasing the G-actin pool available to form branches |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAPZA1 | up-regulates quantity
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261855 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 27871158 |
Finally, the capZ protein recaps the barbed filament ends to complete the assembly and these actin cytoskeletons can be used for cellular contraction, resulting in the final activated platelet shape |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FLNA | up-regulates quantity by stabilization
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261851 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11706047 |
We conclude that FLNa is essential in cells that express it for stabilizing orthogonal actin networks suitable for locomotion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCIN | up-regulates
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268503 |
|
|
Homo sapiens |
Spermatozoon |
| pmid |
sentence |
| 11090452 |
The results suggest that the affinity of calicin to F-actin allows targeting of calicin at the subacrosomal space of round spermatids, and that its ability to form homomultimers contributes to the formation of a rigid calyx. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
F-actin_assembly | down-regulates activity 
relocalization
|
AIIB/b3 integrin |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261864 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27871158 |
Integrin αIIbβ3 is retained by the actin cytoskeleton in resting platelets but is released to the cell surface during platelet activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ARP2/3 | up-regulates quantity
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261838 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 27871158 |
The Arp2/3 complex stimulates the assembly of actin filaments. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | T cell activation |
| + |
OPHN1 | up-regulates
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268400 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 12932438 |
These results based on the immunodetection of the endogenous protein clearly show that OPHN1 colocalizes with F-actin in both neuronal and glial cells and suggest that OPHN-1 interacts with actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CFL1 | down-regulates quantity
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261836 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 27871158 |
Cofilin also binds to actin and contributes to the disassembly of actin filaments and the subsequent release of actin monomers. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
GAS2L1 | up-regulates
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273700 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24706950 |
Previous work has shown that members of the growth-arrest-specific 2 (GAS2) family mediate the crosstalk between filamentous actin (F-actin) and MTs, but the molecular basis of this process remained unclear. By using fluorescence microscopy, we demonstrate that three members of this family, GAS2-like 1, GAS2-like 2 and GAS2-like 3 (G2L1, G2L2 and G2L3, also known as GAS2L1, GAS2L2 and GAS2L3, respectively) are differentially involved in mediating the crosstalk between F-actin and MTs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GAS2 | up-regulates
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273701 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24706950 |
Previous work has shown that members of the growth-arrest-specific 2 (GAS2) family mediate the crosstalk between filamentous actin (F-actin) and MTs, but the molecular basis of this process remained unclear. By using fluorescence microscopy, we demonstrate that three members of this family, GAS2-like 1, GAS2-like 2 and GAS2-like 3 (G2L1, G2L2 and G2L3, also known as GAS2L1, GAS2L2 and GAS2L3, respectively) are differentially involved in mediating the crosstalk between F-actin and MTs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
α-Catenin | up-regulates
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265814 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21255999 |
At its C-terminus, cadherin interacts with β-catenin, which dynamically associates with α-catenin, a direct binding partner of filamentous actin |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
F-actin_assembly | up-regulates
|
Axonal_growth_cone_formation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268387 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 21106647 |
Axon outgrowth and guidance to the proper target requires the coordination of filamentous (F)-actin and microtubules (MTs), the dynamic cytoskeletal polymers that promote shape change and locomotion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
GSN | down-regulates quantity
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261835 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 27871158 |
Gelsolin is an actin binding protein that severs and caps the barbed-end actin filaments to prevent actin monomer exchange upon intracellular calcium increase in the initial step. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACTN1 | up-regulates quantity by stabilization
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261852 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27871158 |
Actin exists in polymer where filamin and α-actinin act as cross-linkers with approximately 1:10 ratios |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
ACTG1 | up-regulates quantity
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261878 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28233384 |
Here, we report the highest resolution, cryo-EM structures of actin filaments with bound ATP analog β,γ-imidoadenosine 5′-triphosphate (AMPPNP) (3.1 Å) and ADP with inorganic phosphate (ADP-Pi) (3.1 Å) as well as a 3.6-Å resolution structure of the ADP filament. These structures of the three well-characterized nucleotide states of actin monomers and filaments |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Erythrocytic spectrin | up-regulates
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266030 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24302288 |
Spectrin is a member of the F-actin-crosslinking protein superfamily. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RHOA | up-regulates
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192114 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23450633 |
Ga12/13 recruitment of rho-gefs causes rhoa activation and f-actin assembly, which promotes lats1/lat2 inactivation by an unknown, but myosin-independent mechanism. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACTB | up-regulates quantity
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261879 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28233384 |
Here, we report the highest resolution, cryo-EM structures of actin filaments with bound ATP analog β,γ-imidoadenosine 5′-triphosphate (AMPPNP) (3.1 Å) and ADP with inorganic phosphate (ADP-Pi) (3.1 Å) as well as a 3.6-Å resolution structure of the ADP filament. These structures of the three well-characterized nucleotide states of actin monomers and filaments |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
F-actin_assembly | down-regulates
|
LATS2 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192783 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23450633 |
Ga12/13 recruitment of rho-gefs causes rhoa activation and f-actin assembly, which promotes lats1/lat2 inactivation by an unknown, but myosin-independent mechanism. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Hippo Signaling |
| + |
CFL2 | down-regulates quantity
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261837 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 27871158 |
Cofilin also binds to actin and contributes to the disassembly of actin filaments and the subsequent release of actin monomers. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
F-actin_assembly