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Luciferase reporter assays confirm MTMR6 as a direct miR (show MYLIP Proteins)-190b target; miR (show MYLIP Proteins)-190b-mediated MTMR6 downregulation suggests an important mechanism that could keep infected cells in an activated state, thereby promoting viral replication.
MTMR6, which dephosphorylates PI(3 (show PI3 Proteins))P to PI, and its binding partner MTMR9 (show MTMR9 Proteins), are required for macropinocytosis.
results indicate that the cellular localization of MTMR6 is regulated by Rab1B (show RAB1B Proteins) in the early secretory and autophagic pathways
investigation of MTM1 (show MTM1 Proteins) and MTMR6 and finding that they use PtdIns(3,5)P2 in addition to PtdIns3P as a substrate in vitro
Identification of myotubularin (show MTM1 Proteins) as the lipid phosphatase catalytic subunit associated with the 3-phosphatase adapter protein (show MTMR12 Proteins), 3-PAP (show MTMR12 Proteins).
Data show that KCa3.1 (show KCNN4 Proteins), which is critical for Ca2 (show CA2 Proteins)+ influx in reactivated naive T cells and central memory T cells, requires phosphatidylinositol-3 phosphatase for activation and is inhibited by PI(3 (show PI3 Proteins))P phosphatase myotubularin-related protein 6 (MTMR6).
MTMR9 (show MTMR9 Proteins) greatly enhances the functions of MTMR6
Phosphatase that acts on lipids with a phosphoinositol headgroup. Acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4+ T-cells possibly by decreasing intracellular levels of phosphatidylinositol 3 phosphatase. Negatively regulates proliferation of reactivated CD4+ T-cells (By similarity).
myotubularin-related protein 6
, myotubularin related protein 6
, myotubularin-related protein 6-like