Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.3.36 extracted from

  • Ijuin, T.; Takenawa, T.
    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) (2012), J. Biol. Chem., 287, 6991-6999.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.36

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
C2C12 cell
-
 Mus musculus
-

Synonyms

Synonyms Comment Organism
SHIP2
-
 Mus musculus
SKIP
-
 Mus musculus

General Information

General Information Comment Organism
malfunction in SHIP2 siRNA transfected cells, insulin treatment does not lead to alter the PIP3 level in contrast to SKIP or PTEN silenced cells. Results demonstrate that SHIP2 in contrast to SKIP is not involved in the regulation of insulin signaling in C2C12 cells Mus musculus
malfunction in SKIP siRNA transfected cells, insulin treatment show an increase in PIP3 compared with control cells. Significant decrease in PI(3,4)P2 level is observed by the silencing of SKIP compared to control cells. PI(3,4)P2 levels are not altered in siRNA-transfected cells. Silencing of SKIP, increases the insulin-dependent recruitment of GLUT4 vesicles to the plasma membrane Mus musculus
metabolism SKIP controls PIP3 content in an insulin stimulation-dependent manner Mus musculus
physiological function SKIP negatively regulates insulin signaling and glucose uptake by inhibiting GLUT4 docking and/or fusion to the plasma membrane Mus musculus