PPP1R9B

protein phosphatase 1 regulatory subunit 9B

Seems to act as a scaffold protein in multiple signaling pathways. Modulates excitatory synaptic transmission and dendritic spine morphology. Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction. Believed to target protein phosphatase 1/PP1 to dendritic spines, which are rich in F-actin, and regulates its specificity toward ion channels and other substrates, such as AMPA-type and NMDA-type glutamate receptors. Plays a role in regulation of G-protein coupled receptor signaling, including dopamine D2 receptors and alpha-adrenergic receptors. May establish a signaling complex for dopaminergic neurotransmission through D2 receptors by linking receptors downstream signaling molecules and the actin cytoskeleton. Binds to ADRA1B and RGS2 and mediates regulation of ADRA1B signaling. May confer to Rac signaling specificity by binding to both, RacGEFs and Rac effector proteins. Probably regulates p70 S6 kinase activity by forming a complex with TIAM1 (By similarity).
Required for hepatocyte growth factor (HGF)-induced cell migration.

Actin filament depolymerizationIEA:Ensembl
Actin filament organizationManual Assertion Based On ExperimentIBA:GO_Central
AgingIEA:Ensembl
Calcium-mediated signalingManual Assertion Based On ExperimentIBA:GO_Central
Cell migrationManual Assertion Based On ExperimentIMP:UniProtKB
Cellular response to epidermal growth factor stimulusIEA:Ensembl
Cellular response to estradiol stimulusIEA:Ensembl
Cellular response to morphineISS:UniProtKB
Cellular response to peptideIEA:Ensembl
Cellular response to xenobiotic stimulusIEA:Ensembl
Cerebral cortex developmentIEA:Ensembl
Dendrite developmentIEA:Ensembl
Developmental process involved in reproductionIEA:Ensembl
Filopodium assemblyManual Assertion Based On ExperimentIMP:UniProtKB
Hippocampus developmentIEA:Ensembl
LearningIEA:Ensembl
Male mating behaviorIEA:Ensembl
Modulation of chemical synaptic transmissionIEA:InterPro
Negative regulation of cell growthManual Assertion Based On ExperimentIDA:UniProtKB
Negative regulation of phosphoprotein phosphatase activityIEA:Ensembl
Neuron projection developmentManual Assertion Based On ExperimentIBA:GO_Central
Positive regulation of protein localization to actin cortical patchIEA:Ensembl
Positive regulation of protein localization to plasma membraneIEA:Ensembl
Protein localization to actin cytoskeletonIEA:Ensembl
Protein localization to cell peripheryIEA:Ensembl
Regulation of cell cycleManual Assertion Based On ExperimentTAS:UniProtKB
Regulation of cell growth by extracellular stimulusManual Assertion Based On ExperimentTAS:UniProtKB
Regulation of cell population proliferation1 PublicationNAS:UniProtKB
Regulation of exit from mitosis1 PublicationNAS:UniProtKB
Regulation of opioid receptor signaling pathwayISS:UniProtKB
Regulation of protein phosphorylationIEA:Ensembl
Reproductive system developmentIEA:Ensembl
Response to amphetamineIEA:Ensembl
Response to clozapineIEA:Ensembl
Response to immobilization stressIEA:Ensembl
Response to kainic acidIEA:Ensembl
Response to L-phenylalanine derivativeIEA:Ensembl
Response to nicotineIEA:Ensembl
Response to prostaglandin EIEA:Ensembl
Response to steroid hormoneIEA:Ensembl
RNA splicing1 PublicationNAS:UniProtKB

Cytoplasm, cytoskeleton
Nucleus
Cell projection, dendritic spine
Postsynaptic density
Synapse
Cell junction, adherens junction
Cytoplasm
Cell membrane
Cell projection, lamellipodium
Cell projection, filopodium
Cell projection, ruffle membrane
Enriched at synapse and cadherin-based cell-cell adhesion sites. In neurons, both cytosolic and membrane-associated, and highly enriched in the postsynaptic density apposed to exitatory synapses. Colocalizes with PPP1R2 at actin-rich adherens junctions in epithelial cells and in dendritic spines (By similarity).
Accumulates in the lamellipodium, filopodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment.

Stimulation of D1 (but not D2) dopamine receptors induces Ser-94 phosphorylation. Dephosphorylation of Ser-94 is mediated mainly by PP1 and to a lesser extent by PP2A. Phosphorylation of spinophilin disrupts its association with F-actin, but does not affect its binding to PP1 (By similarity).