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The protein encoded by FIG4 belongs to the SAC domain-containing protein gene family. Additionally we are shipping FIG4 Antibodies (74) and many more products for this protein.
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Inactivation of Fig4 in motor neurons display neuronal and axonal degeneration.
Fig4 expression in the neurons is both necessary and sufficient to prevent spongiform neurodegeneration
Haploinsufficiency of Fig4 does not impose risks in rodents to develop neuronal degeneration in either naive or traumatic conditions.
Here we provide strong evidence that Mtmr2 (show MTMR2 Proteins) and Fig4 functionally interact in both Schwann cells and neurons, and we reveal for the first time a role of Mtmr2 (show MTMR2 Proteins) in neurons in vivo
Fig4 may be required to prevent neurons and glia from excessive lysosomal accumulation after injury and in neurodegeneration.
Pathogenic mechanism of the FIG4 mutation responsible for Charcot-Marie-Tooth disease CMT4J
Results suggest that Fig4 deficiency affects motor neurons differently from sensory neurons by mechanisms involving excessive retention of molecules in lysosomes or disruption of vacuolated organelles.
a novel regulatory mechanism whereby ArPIKfyve (show VAC14 Proteins) enhances Sac3 abundance by attenuating Sac3 proteasome-dependent degradation and suggest that a failure of this mechanism could be the primary molecular defect in the pathogenesis of CMT4J.
shd1 (show SAC3D1 Proteins) is involved in cell cycle progression, in particular centrosome duplication and a spindle assembly checkpoint function.
Sac3 as an insulin (show INS Proteins)-sensitive phosphatase whose down-regulation increases insulin (show INS Proteins) responsiveness, thus implicating Sac3 as a novel drug target in insulin (show INS Proteins) resistance.
These results suggest that FIG4 binds to hepatitis C virus and modulates particle formation in a cholesteryl ester-related manner.
data identify a novel role of the ArPIKfyve (show VAC14 Proteins)-Sac3 (show MCM3AP Proteins) complex in the mechanisms controlling aggregate formation of Sph1 and suggest that Sac3 (show MCM3AP Proteins) protein deficiency or overproduction may facilitate aggregation of aggregation-prone proteins
The findings suggest that FIG4 may have a common role in the formation or degradation of neuronal cytoplasmic and nuclear inclusions in several neurodegenerative diseases.
FIG4 mutations were identified in autosomal-dominant Amyotrophic lateral sclerosis.
Phenotypes associated with FIG4 mutations include cortical malformation associated with seizures and psychiatric manifestations, in addition to the Charcot-Marie-Tooth disease type 4J and Yunis-Varon syndrome.
Identified novel biallelic FIG4 mutations.
Genetic variations in the FIG4 gene were not found to cause ALS in Italian patients.
results uncover an unexpected role for Sac3 (show MCM3AP Proteins) phosphatase in triple-negative breast cancer cell proliferation
Yunis-Varon syndrome is caused by mutations in FIG4, encoding a phosphoinositide phosphatase.
This study demonistrated that CMT4J is a clinically distinct form of Charcot-Marie-Tooth disease with mutations in the PI(3,5)P phosphatase FIG4.
The protein encoded by this gene belongs to the SAC domain-containing protein gene family. The SAC domain, approximately 400 amino acids in length and consisting of seven conserved motifs, has been shown to possess phosphoinositide phosphatase activity. The yeast homolog, Sac1p, is involved in the regulation of various phosphoinositides, and affects diverse cellular functions such as actin cytoskeleton organization, Golgi function, and maintenance of vacuole morphology. Membrane-bound phosphoinositides function as signaling molecules and play a key role in vesicle trafficking in eukaryotic cells. Mutations in this gene have been associated with Charcot-Marie-Tooth disease, type 4J.
SAC domain-containing protein 3
, Sac domain-containing inositol phosphatase 3
, phosphatidylinositol 3,5-bisphosphate 5-phosphatase
, polyphosphoinositide phosphatase
, FIG4 homolog, SAC domain containing lipid phosphatase
, FIG4 homolog, SAC1 domain containing lipid phosphatase