| + |
ABL2 | up-regulates 
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266594 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 33622779 |
Here, using cultured hippocampal neurons pooled from both sexes of mice, we provide evidence that binding to cortactin tethers Abl2 in spines, where Abl2 and cortactin maintain the small pool of stable actin required for dendritic spine stability. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
Actin_cytoskeleton_reorganization | up-regulates
|
Axonal_growth_cone_formation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268383 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268384 |
|
|
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: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
ACTN1 | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264618 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17243894 |
On most principal neurons in the mammalian brain (e.g., pyramidal neurons of cortex and hippocampus, Purkinje cells of cerebellum, medium spiny neurons of striatum), the postsynaptic specialization is housed on tiny actin rich protrusions called dendritic spines The size, shape, motility, and stability of dendritic spines depend largely on actin, the primary cytoskeleton within spines. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance, Glutamatergic synapse |
| + |
MYO10 | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268283 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27580874 |
Myosin X is required for filopodia formation and extension. myosin X functions as an antiparallel dimer in cells with a unique geometry optimized for movement on actin bundles. Myosin X facilitates initiation and elongation of filopodia, which implies favouring formation of parallel bundled F-actin filaments. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
MAPK8 | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258976 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19279717 |
To date it is not clear whether any genes are transcribed downstream of these two GTPases for non-canonical signaling. The prevailing dogma remains that their primary roles are indeed solely for cytoskeletal modulation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Actin_cytoskeleton_reorganization | up-regulates
|
Dendritic_spine_morphogenesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266596 |
|
|
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 |
| + |
CTTN | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261696 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 23015759 |
Through alternative splicing, a single CTTNBP2 gene encodes three different transcripts, namely short (S), long (L), and intron forms. The interaction with cortactin is required for the function of CTTNBP2-S in dendritic spine formation because the CTTNBP2-S mutant, which no longer interacts with cortactin, is unable to rescue the spine defects resulting from CTTNBP2 knockdown. Thus CTTNBP2-S may control cortactin–F-actin cytoskeletons and regulate the formation and maintenance of dendritic spines in neurons. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PFN1 | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258977 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18667433 |
Additionally, the association of Ror2 with the actin-binding protein filamin A is required for Wnt5a-induced JNK activation and polarized cell migration. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
COMMD5 | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261693 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30021164 |
In this study, we identified a specific and crucial role for COMMD5 in the endocytic trafficking machinery, and especially we determined COMMD5 as an actin- and tubulin-binding protein. Our results provide further insight into the essential role of COMMD5 on every aspect of cellular processes, from membrane receptor trafficking to cytoskeleton organization, cell migration, and junctions. Here, we demonstrate that COMMD5 is crucial for the stability of the cytoskeleton. Its silencing leads to a major re-organization of actin and microtubule networks. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258975 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19279717 |
To date it is not clear whether any genes are transcribed downstream of these two GTPases for non-canonical signaling. The prevailing dogma remains that their primary roles are indeed solely for cytoskeletal modulation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
p38 | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254360 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11591790 |
The p21 G protein Rho and its targets, Rho-associated coiled-coil forming protein kinases (p160ROCK/ROCK I/ROKβ and Rho kinase/ROCK II/ROKα), play a crucial role in actin cytoskeleton reorganization |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ARHGEF6 | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272236 |
|
|
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 23776207 |
Activation of ARF6 promotes cortical actin assembly (9) and plasma membrane remodeling |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYN2 | up-regulates activity 
binding
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269185 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15265865 |
Synapsins, a family of neuron-specific phosphoproteins, have been demonstrated to regulate the availability of synaptic vesicles for exocytosis by binding to both synaptic vesicles and the actin cytoskeleton in a phosphorylation-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LINC complex | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263293 |
|
|
|
|
| pmid |
sentence |
| 24481844 |
The extensive covalent and non-covalent attachments as well as the binding avidity between three KASH domains with three SUN domains are thought to enable the LINC complex to transmit force between the cytoskeleton and the nucleoskeleton |
|
| Publications: |
1 |
| + |
ROCK2 | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261712 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14701738 |
Two functions for Gem have been demonstrated, including inhibition of voltage-gated calcium channel activity and inhibition of Rho kinase-mediated cytoskeletal reorganization, such as stress fiber formation and neurite retraction. These functions for Gem have been ascribed to its interaction with the calcium channel Β subunit and Rho kinase Β, respectively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261722 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14701738 |
Two functions for Gem have been demonstrated, including inhibition of voltage-gated calcium channel activity and inhibition of Rho kinase-mediated cytoskeletal reorganization, such as stress fiber formation and neurite retraction. These functions for Gem have been ascribed to its interaction with the calcium channel Β subunit and Rho kinase Β, respectively. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
NHS | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253565 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20332100 |
We demonstrate that NHS is essential for maintaining cell morphology through the regulation of actin cytoskeletal dynamics and suggest that an important mechanism of remodelling of the actin cytoskeleton during development would therefore be lost in patients with NHS. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TBCK | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266701 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23977024 |
Depletion of TBCK significantly inhibits cell proliferation, reduces cell size, and disrupts the organization of actin, but not microtubule. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTTNBP2NL | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261694 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 23015759 |
Through alternative splicing, a single CTTNBP2 gene encodes three different transcripts, namely short (S), long (L), and intron forms. The interaction with cortactin is required for the function of CTTNBP2-S in dendritic spine formation because the CTTNBP2-S mutant, which no longer interacts with cortactin, is unable to rescue the spine defects resulting from CTTNBP2 knockdown. Thus CTTNBP2-S may control cortactin–F-actin cytoskeletons and regulate the formation and maintenance of dendritic spines in neurons. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
FSCN1 | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268375 |
|
|
Mus musculus |
Glioma Cell |
| pmid |
sentence |
| 21706053 |
Plexin-B3 interacts with the actin-binding protein fascin-1. The present finding suggests fascin-1 as a potential effector of plexin-B3 to mediate the signal of Sema5A in glioma cells.Sema5A and plexin-B3 remodel F-actin cytoskeleton and induce fascin-1 translocation in glioma cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Axon guidance |
| + |
SYN1 | up-regulates activity
binding
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269187 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15265865 |
Synapsins, a family of neuron-specific phosphoproteins, have been demonstrated to regulate the availability of synaptic vesicles for exocytosis by binding to both synaptic vesicles and the actin cytoskeleton in a phosphorylation-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYN3 | up-regulates activity
binding
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269186 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15265865 |
Synapsins, a family of neuron-specific phosphoproteins, have been demonstrated to regulate the availability of synaptic vesicles for exocytosis by binding to both synaptic vesicles and the actin cytoskeleton in a phosphorylation-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
Actin_cytoskeleton_reorganization