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findings underscore the specific and prominent role of SKIP and GRP78 in the regulation of insulin-dependent PI 3-kinase signaling in skeletal muscle
prominent role of SKIP in the development of insulin resistance in skeletal muscle
the physiological role of Pak1-SKIP binding is in the regulation of insulin signaling in skeletal muscle
SKIP controls the IGF-II-PI 3-kinase-Akt-mTOR auto-regulation loop during myogenesis.
Specific suppression of insulin signaling is achieved via the spatiotemporal regulation of SKIP through the scaffolding function of Pak1.
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/aquaporin-2 signalling pathway and water transport in kidney collecting ducts.
Silencer of death domains (SODD) inhibits skeletal muscle and kidney enriched inositol 5-phosphatase (SKIP) and regulates phosphoinositide 3-kinase (PI3K)/Akt signaling to the actin cytoskeleton.
These results imply that SKIP regulates insulin signaling in skeletal muscle.
results suggest that SKIP (skeletal muscle and kidney-enriched inositol phosphatase) plays a negative regulatory role in Akt/ GSK-3beta/GS (glycogen synthase) pathway leading to glycogen synthesis in myocytes
the distribution of genotype frequency exhibited no significant differences between the Parkinson's disease and control groups (P > 0.025) in INPP5K rs1109303 (P = 0.048, OR = 0.806, 95%CI = 0.650 - 0.998).
In individuals exhibiting congenital muscular dystrophy, early-onset cataracts, and mild intellectual disability but normal cranial magnetic resonance imaging, we identified bi-allelic mutations in INPP5K, encoding inositol polyphosphate-5-phosphatase K.
Mutations in INPP5K cause a congenital muscular dystrophy syndrome with short stature, cataracts, and intellectual disability.
These findings suggest a model by which GRP78 regulates intracellular localization of SKIP and how SKIP binds to Pak1 on insulin stimulation.
Study reveals that SKIP is a significant regulator of glioblastoma cell migration and that increased expression of SKIP may confer a survival advantage.
identification of novel domain that mediates membrane ruffle localization
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, 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