Literature DB >> 7897444

Organization of microtubules in myelinating Schwann cells.

G J Kidd1, S B Andrews, B D Trapp.   

Abstract

Myelinating Schwann cells polarize their surface membrane into several ultrastructurally and biochemically distinct domains that constitute the myelin internode. Formation of these membrane domains depends on contact with appropriate axons and requires microtubule-based transport systems for site-specific targeting of membrane components. Because little is known about microtubules in myelinating Schwann cells, this study used confocal microscopy and the microtubule hook-labelling method to characterize microtubule distribution, the location of microtubule nucleation sites, and the polarity and composition of Schwann cell microtubules. In myelinating Schwann cells, microtubules were abundant within the Golgi-rich perinuclear cytoplasm; they were not attached to the centrosome. Three-fourths of the microtubules in the cytoplasmic channels located along the outer perimeter of the myelin internode had their (+) ends oriented away from the perinuclear region, whereas the remaining 25% had the opposite polarity. Depolymerization/repolymerization experiments detected microtubule nucleating sites in perinuclear cytoplasm but not along the myelin internode. Taken together, these results indicate that microtubule-mediated transport of myelin components along the internode could utilize both (+)- and (-)-end motors. Specialized microtubule tracks that target myelin proteins to specific sites were not identified on the basis of tubulin polarity or posttranslational modifications.

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Year:  1994        PMID: 7897444     DOI: 10.1007/bf01268092

Source DB:  PubMed          Journal:  J Neurocytol        ISSN: 0300-4864


  8 in total

1.  Polarity of microtubule assemblies during neuronal cell migration.

Authors:  P Rakic; E Knyihar-Csillik; B Csillik
Journal:  Proc Natl Acad Sci U S A       Date:  1996-08-20       Impact factor: 11.205

2.  Microtubule organization and stability in the oligodendrocyte.

Authors:  K F Lunn; P W Baas; I D Duncan
Journal:  J Neurosci       Date:  1997-07-01       Impact factor: 6.167

3.  A laminin-2, dystroglycan, utrophin axis is required for compartmentalization and elongation of myelin segments.

Authors:  Felipe A Court; Jane E Hewitt; Kay Davies; Bruce L Patton; Antonino Uncini; Lawrence Wrabetz; M Laura Feltri
Journal:  J Neurosci       Date:  2009-03-25       Impact factor: 6.167

4.  Regulatory role of cytochrome P450scc and pregnenolone in myelination by rat Schwann cells.

Authors:  Thant S Zhu; Michael Glaser
Journal:  Mol Cell Biochem       Date:  2008-03-31       Impact factor: 3.396

5.  MMP2-9 cleavage of dystroglycan alters the size and molecular composition of Schwann cell domains.

Authors:  Felipe A Court; Desirée Zambroni; Ernesto Pavoni; Cristina Colombelli; Chiara Baragli; Gianluca Figlia; Lydia Sorokin; William Ching; James L Salzer; Lawrence Wrabetz; M Laura Feltri
Journal:  J Neurosci       Date:  2011-08-24       Impact factor: 6.167

6.  Nonuniform microtubular polarity established by CHO1/MKLP1 motor protein is necessary for process formation of podocytes.

Authors:  N Kobayashi; J Reiser; W Kriz; R Kuriyama; P Mundel
Journal:  J Cell Biol       Date:  1998-12-28       Impact factor: 10.539

Review 7.  Podocytes … What's Under Yours? (Podocytes and Foot Processes and How They Change in Nephropathy).

Authors:  Chris R Neal
Journal:  Front Endocrinol (Lausanne)       Date:  2015-02-23       Impact factor: 5.555

8.  Ribosomal trafficking is reduced in Schwann cells following induction of myelination.

Authors:  James M Love; Sameer B Shah
Journal:  Front Cell Neurosci       Date:  2015-08-19       Impact factor: 5.505

  8 in total

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