+ |
MAPK1 |
phosphorylation
|
PPP1R9B |
0.476 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249435 |
Ser15 |
GPGGPLRsASPHRSA |
Homo sapiens |
|
pmid |
sentence |
15728359 |
We have identified three sites phosphorylated by ERK2 (Ser-15 and Ser-205) and cyclin-dependent PK 5 (Cdk5) (Ser-17), within the actin-binding domain of spinophilin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKACA | down-regulates activity
phosphorylation
|
PPP1R9B |
0.314 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250035 |
Ser94 |
SERGVRLsLPRASSL |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
12417592 |
Spinophilin is phosphorylated in vitro by protein kinase A (PKA). two major sites of phosphorylation, Ser-94 and Ser-177, that are located within the actin-binding domain of spinophilin. Phosphorylation of spinophilin by PKA modulated the association between spinophilin and the actin cytoskeleton. phosphorylation of spinophilin reduced the stoichiometry of the spinophilin-actin interaction. In contrast, the ability of spinophilin to bind to PP1 remained unchanged. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1R9B | up-regulates activity
binding
|
SPATA13 |
0.496 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269174 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19151759 |
Here we show that Asef2, but not Asef, interacts with Neurabin2/Spinophilin, a scaffold protein that binds to Filamentous actin (F-actin). Neurabin2 is required for Asef2-induced filopodia formation. RNA interference experiments showed that Asef2, Neurabin2 and APC are involved in HGF-induced cell migration. Furthermore, knockdown of Neurabin2 resulted in the suppression of Asef2-induced filopodia formation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1R9B | up-regulates quantity
binding
|
TIAM1 |
0.433 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269175 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
12531897 |
Spinophilin binding promotes the plasma membrane localization of Tiam1 and enhances the ability of Tiam1 to activate p70 S6 kinase. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
PPP1R9B | up-regulates activity
binding
|
ARHGEF2 |
0.405 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269176 |
|
|
Mus musculus |
Neuro-2a Cell |
pmid |
sentence |
15996550 |
The Rho Family GEF Lfc Interacts with Neurabin and Spinophilin. Neurabin and spinophilin are homologous protein phosphatase 1 and actin binding proteins that regulate dendritic spine function. 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 |
+ |
PPP1R9B | up-regulates activity
binding
|
PP1 |
0.764 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269178 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
10194355 |
In the present study, the interaction between PP1 and spinophilin, a neuronal protein that targets PP1 to dendritic spines, has been characterized. . These studies support the notion that spinophilin functions in vivo as a neuronal PP1 targeting subunit by directing the enzyme to postsynaptic densities and regulating its activity toward physiological substrates. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
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 |