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Switch #:
SWTI000194
Switch type:
Binary
Switch subtype:
Physicochemical compatibility

Description:
Phosphorylation of S385 adjacent to the cleavage motif of Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (PTEN) by CK2 subfamily prevents cleavage by Caspase-3 (CASP3).

Participants:
(1) Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (PTEN)
(2) Caspase-3 (CASP3)

Interactions
Interaction #1 PTEN - CASP3

Interfaces
(1) CLV_C14_Caspase3-7 motif (381DTTDS385) in Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (PTEN)
(2) Caspase domain (45-275) in Caspase-3 (CASP3)

Interaction Regulation
PTM-dependent Abrogation (Phosphorylation of S385 on Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (PTEN)) of the Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (PTEN) CLV_C14_Caspase3-7 motif - Caspase-3 (CASP3) Caspase domain interaction

Regulatory Enzymes for switch
Modifying enzymes for residue: S385: CK2 subfamily

Inferred Regulatory Enzymes for switch
Putative modifying enzymes for residue: S385 : CK2_group, Casein kinase II subunit alpha (CSNK2A1).

Context
Switch localisation
ELM curated: cytosol, nucleus
Inferred: cytosol


Switch pathways
Inferred: p53 signaling pathway
References

(1) Phosphorylation-regulated cleavage of the tumor suppressor PTEN by caspase-3: implications for the control of protein stability and PTEN-protein interactions.
Torres et al. J. Biol. Chem. (2003)

See also

Other switches involving participants
Caspase-3 (CASP3) - 2 more (view)

Other switches involving interfaces
Caspase domain - 3 more (view)
CLV_C14_Caspase3-7 - 1 more (view)


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