Differential and cell development-dependent localization of myelin mRNAs in oligodendrocytes

Vries, H. de; Jonge, Jenny C. de; Schrage, C; Haar, Marjan E. van der; Hoekstra, Dick

doi:10.1002/(sici)1097-4547(19970301)47:5<479::aid-jnr3>3.0.co;2-e

Cited by 44 publications

(36 citation statements)

References 27 publications

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“…Expression of these isoforms is developmentally regulated and they have different locations in cells and myelin, suggesting that they may have different functions. The isoforms containing the exon II-encoded domain are expressed at high levels early in myelination and in immature OLs in culture [42,45,46], while the forms lacking this domain are the primary forms expressed later in myelination, in mature OLs, and in adult myelin. Although the 18.5-kDa form is the primary form in adult human myelin, exon II-containing forms are expressed during fetal development and during remyelination [41].…”

Section: Size Isoforms Of Mbpmentioning

confidence: 99%

Myelin basic protein: a multifunctional protein

Boggs

2006

Cell. Mol. Life Sci.

577

558

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Myelin basic protein (MBP), the second most abundant protein in central nervous system myelin, is responsible for adhesion of the cytosolic surfaces of multilayered compact myelin. A member of the 'intrinsically disordered' or conformationally adaptable protein family, it also appears to have several other functions. It can interact with a number of polyanionic proteins including actin, tubulin, Ca(2+)-calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. Some size isoforms of MBP are transported into the nucleus and thus they may also bind polynucleotides. Extracellular signals received by myelin or cultured oligodendrocytes cause changes in phosphorylation of MBP, suggesting that MBP is also involved in signaling. Further study of this very abundant protein will reveal how it is utilized by the oligodendrocyte and myelin for different purposes.

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Section: Size Isoforms Of Mbpmentioning

confidence: 99%

Myelin basic protein: a multifunctional protein

Boggs

2006

Cell. Mol. Life Sci.

577

558

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“…Fixation of cells for immunofluorescence was as described by de Vries et al (1997), using 4% paraformaldehyde fixation for 20 min and 0.1% TX-100 permeabilization for 30 min. Antibodies were diluted to appropriate concentrations.…”

Section: Immunocytochemistrymentioning

confidence: 99%

An Apical-Type Trafficking Pathway Is Present in Cultured Oligodendrocytes but the Sphingolipid-enriched Myelin Membrane Is the Target of a Basolateral-Type Pathway

Vries

Schrage

Hoekstra

1998

MBoC

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Myelin sheets originate from distinct areas at the oligodendrocyte (OLG) plasma membrane and, as opposed to the latter, myelin membranes are relatively enriched in glycosphingolipids and cholesterol. The OLG plasma membrane can therefore be considered to consist of different membrane domains, as in polarized cells; the myelin sheet is reminiscent of an apical membrane domain and the OLG plasma membrane resembles the basolateral membrane. To reveal the potentially polarized membrane nature of OLG, the trafficking and sorting of two typical markers for apical and basolateral membranes, the viral proteins influenza virus-hemagglutinin (HA) and vesicular stomatitis virus-G protein (VSVG), respectively, were examined. We demonstrate that in OLG, HA and VSVG are differently sorted, which presumably occurs upon their trafficking through the Golgi. HA can be recovered in a Triton X-100-insoluble fraction, indicating an apical raft type of trafficking, whereas VSVG was only present in a Triton X-100-soluble fraction, consistent with its basolateral sorting. Hence, both an apical and a basolateral sorting mechanism appear to operate in OLG. Surprisingly, however, VSVG was found within the myelin sheets surrounding the cells, whereas HA was excluded from this domain. Therefore, despite its raft-like transport, HA does not reach a membrane that shows features typical of an apical membrane. This finding indicates either the uniqueness of the myelin membrane or the requirement of additional regulatory factors, absent in OLG, for apical delivery. These remarkable results emphasize that polarity and regulation of membrane transport in cultured OLG display features that are quite different from those in polarized cells.

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“…The regulation of MBP isoforms, and the shift in isoform expression, and thus intracellular localization, may play a key developmental role in oligodendrocyte differentiation [46,47]. The exon-II-containing 21.5-kDa and 17.22-kDa MBP isoforms, and possibly specific isoforms of myelin oligodendrocyte basic protein (MOBP), may also have specific functional, not solely structural, roles in the radial component of mature myelin (see [29]).…”

Section: Resultsmentioning

confidence: 99%

The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal

Smith

Seymour

Boggs

et al. 2012

Biochemical and Biophysical Research Communications

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The predominant 18.5-kDa classic myelin basic protein (MBP) is mainly responsible for compaction of the myelin sheath in the central nervous system, but is multifunctional, having numerous interactions with Ca 2+ -calmodulin, actin, tubulin, and SH3-domains, and can tether these proteins to a lipid membrane in vitro. The full-length 21.5-kDa MBP isoform has an additional 26 residues encoded by exon-II of the classic gene, which causes it to be trafficked to the nucleus of oligodendrocytes (OLGs). We have performed site-directed mutagenesis of selected residues within this segment in red fluorescent protein (RFP)-tagged constructs, which were then transfected into the immortalized N19-OLG cell line to view protein localization using epifluorescence microscopy. We found that 21.5-kDa MBP contains two nontraditional PYnuclear-localization signals, and that arginine and lysine residues within these motifs were involved in subcellular trafficking of this protein to the nucleus, where it may have functional roles during myelinogenesis.

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Differential and cell development-dependent localization of myelin mRNAs in oligodendrocytes

Cited by 44 publications

References 27 publications

Myelin basic protein: a multifunctional protein

Myelin basic protein: a multifunctional protein

An Apical-Type Trafficking Pathway Is Present in Cultured Oligodendrocytes but the Sphingolipid-enriched Myelin Membrane Is the Target of a Basolateral-Type Pathway

The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal

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