PI(3,5)P2 is dephosphorylated to PI5P by the MTMR2:SBF2 tetramer at the plasma membrane

Stable Identifier
R-HSA-6809944
Type
Reaction [transition]
Species
Homo sapiens
Compartment
plasma membrane, cytosol
ReviewStatus
5/5
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PI(3,5)P2 is dephosphorylated to PI5P by the MTMR2:SBF2 tetramer at the plasma membrane
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Formation of a complex with SBF2 (MTMR13) dramatically increases phosphatidylinositol-(3,5)-bisphosphate 3-phosphatase catalytic activity of MTMR2. Since SBF2 sequesters MTRM2 from endosome membranes, the MTMR2 presumably acts on the plasma membrane-associated substrate (Berger et al. 2006).
Literature References
PubMed ID Title Journal Year
16399794 Multi-level regulation of myotubularin-related protein-2 phosphatase activity by myotubularin-related protein-13/set-binding factor-2

Berger, P, Berger, I, Schaffitzel, C, Tersar, K, Volkmer, B, Suter, U

Hum. Mol. Genet. 2006
Participants
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Output
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as an event of
Catalyst Activity

phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity of MTMR2:SBF2 Tetramer [cytosol]

Physical Entity
MTMR2:SBF2 Tetramer [cytosol] (Homo sapiens)
Activity
phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity (GO:0052629)
Inferred From
PI(3,5)P2 is dephosphorylated to PI5P by the Mtmr2:Sbf2 tetramer at the plasma membrane (Mus musculus)
Cross References
RHEA
Authored
Orlic-Milacic, M  (2015-11-13)
Reviewed
Rush, MG  (2017-01-10)
Created
Orlic-Milacic, M  (2015-11-13)
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