Switch #:
SWTI000325
Switch type:
Specificity
Switch subtype:
Domain hiding

Description:
PIP3 (1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate), a product of PI3-kinase, binds to the SH2 domains of PI3K (Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1)) and thereby blocks its interaction with tyrosine-phosphorylated SH2 motif containing proteins.

Participants:
(1) 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
(2) Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1)
(3) Insulin receptor (INSR)

Interactions
Interaction #1 INSR - PIK3R1

Is mutually exclusive with Interaction #2 INSR - PIK3R1

Interfaces
(1) 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
(2) SH2 domain (624-698) in Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1)
Interaction #2 INSR - PIK3R1

Is mutually exclusive with Interaction #1 - - PIK3R1

Interfaces
(3) LIG_SH2_STAT5 motif (1361YTHM1364) in Insulin receptor (INSR)
(4) SH2 domain (624-698) in Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1)

Interaction Regulation
Effector binding Abrogation (1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate) of the Insulin receptor (INSR) LIG_SH2_STAT5 motif - Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1) SH2 domain interaction

Context
Switch localisation
ELM curated: cytosol


Switch pathways
Inferred: PI3K-Akt signaling pathway, Aldosterone-regulated sodium reabsorption, HIF-1 signaling pathway, Insulin signaling pathway
References

(1) Phosphatidylinositol (3,4,5)P3 interacts with SH2 domains and modulates PI 3-kinase association with tyrosine-phosphorylated proteins.
Rameh et al. Cell (1995)




Loading visualisation

↑