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      NF-M is an essential target for the myelin-directed “outside-in” signaling cascade that mediates radial axonal growth

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          Abstract

          Neurofilaments are essential for acquisition of normal axonal calibers. Several lines of evidence have suggested that neurofilament-dependent structuring of axoplasm arises through an “outside-in” signaling cascade originating from myelinating cells. Implicated as targets in this cascade are the highly phosphorylated KSP domains of neurofilament subunits NF-H and NF-M. These are nearly stoichiometrically phosphorylated in myelinated internodes where radial axonal growth takes place, but not in the smaller, unmyelinated nodes. Gene replacement has now been used to produce mice expressing normal levels of the three neurofilament subunits, but which are deleted in the known phosphorylation sites within either NF-M or within both NF-M and NF-H. This has revealed that the tail domain of NF-M, with seven KSP motifs, is an essential target for the myelination-dependent outside-in signaling cascade that determines axonal caliber and conduction velocity of motor axons.

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          Most cited references45

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          Characterization of a cis-Golgi matrix protein, GM130

          Antisera raised to a detergent- and salt-resistant matrix fraction from rat liver Golgi stacks were used to screen an expression library from rat liver cDNA. A full-length clone was obtained encoding a protein of 130 kD (termed GM130), the COOH-terminal domain of which was highly homologous to a Golgi human auto-antigen, golgin-95 (Fritzler et al., 1993). Biochemical data showed that GM130 is a peripheral cytoplasmic protein that is tightly bound to Golgi membranes and part of a larger oligomeric complex. Predictions from the protein sequence suggest that GM130 is an extended rod-like protein with coiled-coil domains. Immunofluorescence microscopy showed partial overlap with medial- and trans-Golgi markers but almost complete overlap with the cis-Golgi network (CGN) marker, syntaxin5. Immunoelectron microscopy confirmed this location showing that most of the GM130 was located in the CGN and in one or two cisternae on the cis-side of the Golgi stack. GM130 was not re-distributed to the ER in the presence of brefeldin A but maintained its overlap with syntaxin5 and a partial overlap with the ER- Golgi intermediate compartment marker, p53. Together these results suggest that GM130 is part of a cis-Golgi matrix and has a role in maintaining cis-Golgi structure.
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            P75 interacts with the Nogo receptor as a co-receptor for Nogo, MAG and OMgp.

            In inhibiting neurite outgrowth, several myelin components, including the extracellular domain of Nogo-A (Nogo-66), oligodendrocyte myelin glycoprotein (OMgp) and myelin-associated glycoprotein (MAG), exert their effects through the same Nogo receptor (NgR). The glycosyl phosphatidylinositol (GPI)-anchored nature of NgR indicates the requirement for additional transmembrane protein(s) to transduce the inhibitory signals into the interior of responding neurons. Here, we demonstrate that p75, a transmembrane protein known to be a receptor for the neurotrophin family of growth factors, specifically interacts with NgR. p75 is required for NgR-mediated signalling, as neurons from p75 knockout mice are no longer responsive to myelin and to each of the known NgR ligands. Blocking the p75-NgR interaction also reduces the activities of these inhibitors. Moreover, a truncated p75 protein lacking the intracellular domain, when overexpressed in primary neurons, attenuates the same set of inhibitory activities, suggesting that p75 is a signal transducer of the NgR-p75 receptor complex. Thus, interfering with p75 and its downstream signalling pathways may allow lesioned axons to overcome most of the inhibitory activities associated with central nervous system myelin.
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              Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells.

              Studies in Trembler and control mice demonstrated that myelinating Schwann cells exert a profound influence on axons. Extensive contacts between myelin and axons have been considered structural. However, demyelination decreases neurofilament phosphorylation, slow axonal transport, and axonal diameter, as well as significantly increasing neurofilament density. In control sciatic nerves with grafted Trembler nerve segments, these changes were spatially restricted: they were confined to axon segments without normal myelination. Adjacent regions of the same axons had normal diameters, neurofilament phosphorylation, cytoskeletal organization, and axonal transport rates. Close intercellular contacts between myelinating Schwann cells and axons modulate a kinase-phosphatase system acting on neurofilaments and possibly other substrates. Myelination by Schwann cells sculpts the axon-altering functional architecture, electrical properties, and neuronal morphologies.
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                Author and article information

                Journal
                J Cell Biol
                The Journal of Cell Biology
                The Rockefeller University Press
                0021-9525
                1540-8140
                8 December 2003
                : 163
                : 5
                : 1011-1020
                Affiliations
                [1 ]Ludwig Institute for Cancer Research, University of California at San Diego, La Jolla, CA 92093
                [2 ]Department of Cellular and Molecular Medicine, University of California at San Diego, La Jolla, CA 92093
                [3 ]Department of Neuroscience, University of California at San Diego, La Jolla, CA 92093
                [4 ]National Center for Microscopy and Imaging Research, University of California at San Diego, La Jolla, CA 92093
                [5 ]Department of Pathology, University of California at San Diego, La Jolla, CA 92093
                [6 ]Howard Hughes Medical Institute, University of California at San Diego, La Jolla, CA 92093
                [7 ]Department of Neurology, Johns Hopkins University School of Medicine, Baltimore, MD 21205
                [8 ]Laboratory of Cell Biology, College of Nutrition, Koshien University, Hyogo 665-0006, Japan
                [9 ]Department of Cell Biology and Neurosciences, Osaka University Graduate School of Medicine, Osaka 565-0871, Japan
                Author notes

                Address correspondence to Don W. Cleveland, Ludwig Institute for Cancer Research, CMM-E/Room 3080, 9500 Gilman Drive, La Jolla, CA 92093-0670. Tel.: (858) 534-7811. Fax: (858) 534-7659. email: dcleveland@ 123456ucsd.edu

                Article
                200308159
                10.1083/jcb.200308159
                2173620
                14662745
                4cc1e835-9ba5-4634-a9f3-38e786f08e74
                Copyright © 2003, The Rockefeller University Press
                History
                : 28 August 2003
                : 14 October 2003
                Categories
                Article

                Cell biology
                myelin; neurofilaments; phosphorylation; axon caliber; radial growth
                Cell biology
                myelin; neurofilaments; phosphorylation; axon caliber; radial growth

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