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report the case of a Charcot-Marie-Tooth type 4B1 patient with a novel mutation in the MTMR2 gene (nonsense mutation in exon 6c.484 C>T; p.Arg162*) who started to experience stridor and was diagnosed with bilateral vocal cord paralysis at the age of 18 months - case report and review
Expression of several MTMR2 isoforms ameliorates the myopathic phenotype owing to MTM1 loss, with increased muscle force, reduced myofiber atrophy, and reduction of the intracellular disorganization hallmarks associated with myotubular myopathy.
The expression of the endogenous transcript is induced in a heterologous cell line by ectopically expressing SOX10, and is nearly ablated in Schwann cells by impairing SOX10 function. Intriguingly, overexpressing the two MTMR2 protein isoforms in HeLa cells revealed that both localize to nuclear puncta and the shorter isoform displays higher nuclear localization compared to the longer isoform
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-mediated differential phosphorylation events.
Mutations in LITAF, RAB7, LMNA, and MTMR2 genes are rare in Chinese Charcot-Marie-Tooth disease (CMT) patients.
Novel mutations in the PRX 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 and MTMR3
REVIEW : MTMR2 belongs to the myotubularin 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-kinase class III complex
A homozygous cytosine to thymine missense mutation at nucleotide position 847, resulting in an amino acid substitution of arginine to tryptophan at codon 283, was detected in exon 9 of the MTMR2 gene
MTMR2 interacts with MTMR5 via its coiled-coil domain and that mutations in the coiled-coil domain of either MTMR2 or MTMR5 abrogate this interaction.
crystal structure of MTMR2, a protein tyrosine phosphatase that is a member of the myotubularin-related protein family.
Loss of MTMR13 (SBF2) function in Charcot-Marie-Tooth disease type 4B patients may lead to alterations in MTMR2 function and subsequent alterations in 3-phosphoinositide signaling.
analysis of the molecular basis for this unique substrate specificity of human myotubularin-related protein-2 (MTMR2) in complex with phosphoinositides
review of the role of MTMR2 and MTMR13 and their involvement in the biology of Schwann cell and CMT4B neuropathies
analysis of epistasis between Mtm1 and Dnm2 reveal possibilities for DNM2 knockdown as a therapeutic approach for X-linked centronuclear myopathy (XLCNM), or myotubular myopathy
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 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 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) with the Sec8 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