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INPP5K encodes a protein with 5-phosphatase activity toward polyphosphate inositol. Additionally we are shipping INPP5K Antibodies (26) and many more products for this protein.
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the physiological role of Pak1 (show PAK1 Proteins)-SKIP binding is in the regulation of insulin (show INS Proteins) signaling in skeletal muscle
SKIP controls the IGF-II-PI 3 (show PI3 Proteins)-kinase-Akt (show AKT1 Proteins)-mTOR (show FRAP1 Proteins) auto-regulation loop during myogenesis.
Specific suppression of insulin (show INS Proteins) signaling is achieved via the spatiotemporal regulation of SKIP through the scaffolding function of Pak1 (show PAK1 Proteins).
Regulation of insulin signaling and glucose transporter 4 (GLUT4) exocytosis by phosphatidylinositol 3,4,5-trisphosphate (PIP3) phosphatase, skeletal muscle, and kidney enriched inositol polyphosphate phosphatase (SKIP).
Results indicate that Inpp5k 5-phosphatase is important for the control of the arginine vasopressin (show AVP Proteins)/aquaporin-2 (show AQP2 Proteins) signalling pathway and water transport in kidney collecting ducts.
Silencer of death domains (SODD (show BAG4 Proteins)) inhibits skeletal muscle and kidney enriched inositol 5-phosphatase (SKIP) and regulates phosphoinositide 3-kinase (PI3K)/Akt (show AKT1 Proteins) signaling to the actin cytoskeleton.
Data shoe that the N-terminal domain of SifA is sufficient to interact with the pleckstrin (show PLEK Proteins) homology domain of SKIP, forming a 1:1 complex with a micromolar dissociation constant.
These results imply that SKIP regulates insulin (show INS Proteins) signaling in skeletal muscle.
results suggest that SKIP (skeletal muscle and kidney-enriched inositol phosphatase) plays a negative regulatory role in Akt (show AKT1 Proteins)/ GSK-3beta/GS (glycogen synthase) pathway leading to glycogen (show GYS1 Proteins) synthesis in myocytes
These findings suggest a model by which GRP78 (show HSPA5 Proteins) regulates intracellular localization of SKIP and how SKIP binds to Pak1 (show PAK1 Proteins) on insulin (show INS Proteins) stimulation.
The authors report that HBV core protein interacts with a cellular SKIP (skeletal muscle and kidney enriched inositol phosphatase) protein, an endoplasmic reticulum-located phosphoinositide 5-phosphatase (show INPP5B Proteins), both in vivo and in vitro.
This gene encodes a protein with 5-phosphatase activity toward polyphosphate inositol. The protein localizes to the cytosol in regions lacking actin stress fibers. It is thought that this protein may negatively regulate the actin cytoskeleton. Alternatively spliced transcript variants encoding different isoforms have been identified.
, inositol polyphosphate 5-phosphatase K
, putative phosphoinositide 5-phosphatase type II
, putative phosphoinositide 5-phosphatase type II; C62
, skeletal muscle and kidney enriched inositol phosphatase
, PI-5-phosphatase related
, putative PI-5-phosphatase
, skeletal muscle and kidney enriched inositol polyphosphate phosphatase
, skeletal muscle and kidney-enriched inositol phosphatase