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MTMR2 is a member of the myotubularin family of phosphoinositide lipid phosphatases. Additionally we are shipping Myotubularin Related Protein 2 Antibodies (51) and many more products for this protein.
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we identified a novel mutation in MTMR2 in a family with CMT4B1 and myelin outfoldings
these results reveal that MTMR2 compartmentalization and potential subsequent effects on endosome maturation and endosome signaling are dynamically regulated through MAPK (show MAPK1 Proteins)-mediated differential phosphorylation events.
Mutations in LITAF (show LITAF Proteins), RAB7 (show RAB7B Proteins), LMNA (show LMNA Proteins), and MTMR2 genes are rare in Chinese Charcot-Marie-Tooth disease (CMT) patients.
Novel mutations in the PRX (show PRDX6 Proteins) and the MTMR2 genes are responsible for unusual Charcot-Marie-Tooth disease phenotypes.
MTMR2 phosphorylation is likely to be a critical mechanism by which MTMR2 access to its lipid substrate(s) is temporally and spatially regulated, thereby contributing to the control of downstream endosome maturation events.
MTMR2 shares similar phosphatase activity and substrate specificity than its homologous proteins MTM1 (show MTM1 Proteins) and MTMR3 (show MTMR3 Proteins)
REVIEW : MTMR2 belongs to the myotubularin (show MTM1 Proteins) family of phosphoinositides phosphatases
Loss of MTMR2, by decreasing Schwann cells proliferation and survival, may impair the first stages of myelination of the peripheral nervous system
REVIEW : MTMR2 and homologous proteins are mutated in several neuromuscular diseases
A phylogenetic study revealing co-evolution of myotubularins with PI 3 (show PI3 Proteins)-kinase class III complex
Mtmr2 and Mtmr13 depend upon each other to achieve wild-type levels of protein expression. Mtmr2 stabilizes Mtmr13 on membranes, indicating that the Mtmr13 pseudophosphatase is regulated by its catalytically active binding partner.
data indicate that Mtmr2 and Mtmr13/Sbf2 play critical roles in the sorting and modulation of cellular signalling which are likely to be disturbed in Charcot-Marie-Tooth disease type 4B
Here we provide strong evidence that Mtmr2 and Fig4 (show FIG4 Proteins) functionally interact in both Schwann cells and neurons, and we reveal for the first time a role of Mtmr2 in neurons in vivo
Loss of phosphatase activity in myotubularin-related protein 2 is associated with Charcot-Marie-Tooth disease type 4B1
Mtmr2 forms a dimer and the C-terminal coiled-coil is responsible for homodimerization, in addition to membrane association
Schwann cell-autonomous loss of Mtmr2-Dlg1 (show DLG1 Proteins) interaction dysregulates membrane homeostasis in the paranodal region, thereby producing outfolding and recurrent loops of myelin.
Loss of Mtmr2 in Schwann cells, but not in motor neurons, is both sufficient and necessary to cause Charcot-Marie-Tooth type neuropaathy.
Interaction of Discs large 1 (Dlg1 (show DLG4 Proteins)) with the Sec8 (show EXOC4 Proteins) exocyst component promotes membrane addition, whereas with Mtmr2, negatively regulates membrane formation.
This gene is a member of the myotubularin family of phosphoinositide lipid phosphatases. The encoded protein possesses phosphatase activity towards phosphatidylinositol-3-phosphate and phosphatidylinositol-3,5-bisphosphate. Mutations in this gene are a cause of Charcot-Marie-Tooth disease type 4B, an autosomal recessive demyelinating neuropathy. Alternatively spliced transcript variants encoding multiple isoforms have been found for this gene.
myotubularin related protein 2
, myotubularin-related protein 2
, myotubularin-related protein 2-like
, Myotubularin-related protein 2