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      A missense mutation in Tbce causes progressive motor neuronopathy in mice.

      Nature genetics
      Amino Acid Sequence, Animals, Axons, metabolism, Blotting, Northern, COS Cells, Chromosome Mapping, Cranial Nerve Diseases, genetics, Crosses, Genetic, DNA Mutational Analysis, Genetic Vectors, HeLa Cells, Humans, In Situ Hybridization, Mice, Mice, Transgenic, Microscopy, Fluorescence, Molecular Chaperones, physiology, Molecular Sequence Data, Mutation, Mutation, Missense, RNA, Messenger, Time Factors, Transfection

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          Abstract

          Mice that are homozygous with respect to the progressive motor neuronopathy (pmn) mutation (chromosome 13) develop a progressive caudio-cranial degeneration of their motor axons from the age of two weeks and die four to six weeks after birth. The mutation is fully penetrant, and expressivity does not depend on the genetic background. Based on its pathological features, the pmn mutation has been considered an excellent model for the autosomal recessive proximal childhood form of spinal muscular atrophy (SMA). Previously, we demonstrated that the genes responsible for these disorders were not orthologous. Here, we identify the pmn mutation as resulting in a Trp524Gly substitution at the last residue of the tubulin-specific chaperone e (Tbce) protein that leads to decreased protein stability. Electron microscopy of the sciatic and phrenic nerves of affected mice showed a reduced number of microtubules, probably due to defective stabilization. Transgenic complementation with a wildtype Tbce cDNA restored a normal phenotype in mutant mice. Our observations indicate that Tbce is critical for the maintenance of microtubules in mouse motor axons, and suggest that altered function of tubulin cofactors might be implicated in human motor neuron diseases.

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          • Record: found
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          Microtubule organization and dynamics dependent on microtubule-associated proteins.

          High-resolution microscopic analysis has precisely revealed the control of microtubule dynamics by individual microtubule-associated proteins (MAPs) in vitro. Furthermore, transfection of MAP cDNA into fibroblasts and subsequent analysis using microinjection of caged fluorescein-labeled tubulin and photoactivation have enabled the function of MAPs in microtubule dynamics to be studied in detail in vivo. Systematic, quantitative studies using transfection of various kinds of MAP cDNA deletion mutants have demonstrated the complex mechanism for microtubule bundling in vivo, and have shown the involvement in microtubule bundling of both microtubule binding and projection regions of MAPs. A similar approach, combined with detailed structural analysis, has indicated clearly that differences in the amino-terminal projection region of MAPs can determine differential organization of MT bundles, and thus influence the characteristic organization of microtubule domains in dendrites and axons.
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            • Record: found
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            Synaptotrophic effects of human amyloid β protein precursors in the cortex of transgenic mice

              Bookmark
              • Record: found
              • Abstract: not found
              • Article: not found

              Pathway Leading to Correctly Folded β-Tubulin

                Bookmark

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