Research ExplorerPublicationsThe raft-associated protein MAL is required for maintenance ...

The raft-associated protein MAL is required for maintenance of proper axon--glia interactions in the central nervous system

Standard

The raft-associated protein MAL is required for maintenance of proper axon--glia interactions in the central nervous system. / Schaeren-Wiemers, Nicole; Bonnet, Annick; Erb, Michael; Erne, Beat; Bartsch, Udo; Kern, Frances; Mantei, Ned; Sherman, Diane; Suter, Ueli.

In: J CELL BIOL, Vol. 166, No. 5, 30.08.2004, p. 731-42.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Schaeren-Wiemers, N, Bonnet, A, Erb, M, Erne, B, Bartsch, U, Kern, F, Mantei, N, Sherman, D & Suter, U 2004, 'The raft-associated protein MAL is required for maintenance of proper axon--glia interactions in the central nervous system', J CELL BIOL, vol. 166, no. 5, pp. 731-42. https://doi.org/10.1083/jcb.200406092

APA

Schaeren-Wiemers, N., Bonnet, A., Erb, M., Erne, B., Bartsch, U., Kern, F., Mantei, N., Sherman, D., & Suter, U. (2004). The raft-associated protein MAL is required for maintenance of proper axon--glia interactions in the central nervous system. J CELL BIOL, 166(5), 731-42. https://doi.org/10.1083/jcb.200406092

Vancouver

Schaeren-Wiemers N, Bonnet A, Erb M, Erne B, Bartsch U, Kern F et al. The raft-associated protein MAL is required for maintenance of proper axon--glia interactions in the central nervous system. J CELL BIOL. 2004 Aug 30;166(5):731-42. https://doi.org/10.1083/jcb.200406092

Bibtex

@article{9fad46efdb4f44da95f6a2edee8f3346,
title = "The raft-associated protein MAL is required for maintenance of proper axon--glia interactions in the central nervous system",
abstract = "The myelin and lymphocyte protein (MAL) is a tetraspan raft-associated proteolipid predominantly expressed by oligodendrocytes and Schwann cells. We show that genetic ablation of mal resulted in cytoplasmic inclusions within compact myelin, paranodal loops that are everted away from the axon, and disorganized transverse bands at the paranode--axon interface in the adult central nervous system. These structural changes were accompanied by a marked reduction of contactin-associated protein/paranodin, neurofascin 155 (NF155), and the potassium channel Kv1.2, whereas nodal clusters of sodium channels were unaltered. Initial formation of paranodal regions appeared normal, but abnormalities became detectable when MAL started to be expressed. Biochemical analysis revealed reduced myelin-associated glycoprotein, myelin basic protein, and NF155 protein levels in myelin and myelin-derived rafts. Our results demonstrate a critical role for MAL in the maintenance of central nervous system paranodes, likely by controlling the trafficking and/or sorting of NF155 and other membrane components in oligodendrocytes.",
keywords = "Animals, Axons, Cell Adhesion Molecules, Cell Communication, Central Nervous System, Down-Regulation, Kv1.2 Potassium Channel, Membrane Microdomains, Membrane Transport Proteins, Mice, Mice, Knockout, Microscopy, Electron, Myelin Basic Protein, Myelin Proteins, Myelin Sheath, Myelin and Lymphocyte-Associated Proteolipid Proteins, Myelin-Associated Glycoprotein, Nerve Growth Factors, Neural Conduction, Oligodendroglia, Optic Nerve, Potassium Channels, Potassium Channels, Voltage-Gated, Protein Transport, Proteolipids, Ranvier's Nodes, Sciatic Nerve, Journal Article, Research Support, Non-U.S. Gov't",
author = "Nicole Schaeren-Wiemers and Annick Bonnet and Michael Erb and Beat Erne and Udo Bartsch and Frances Kern and Ned Mantei and Diane Sherman and Ueli Suter",
year = "2004",
month = aug,
day = "30",
doi = "10.1083/jcb.200406092",
language = "English",
volume = "166",
pages = "731--42",
journal = "J CELL BIOL",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "5",

}

RIS

TY - JOUR

T1 - The raft-associated protein MAL is required for maintenance of proper axon--glia interactions in the central nervous system

AU - Schaeren-Wiemers, Nicole

AU - Bonnet, Annick

AU - Erb, Michael

AU - Erne, Beat

AU - Bartsch, Udo

AU - Kern, Frances

AU - Mantei, Ned

AU - Sherman, Diane

AU - Suter, Ueli

PY - 2004/8/30

Y1 - 2004/8/30

N2 - The myelin and lymphocyte protein (MAL) is a tetraspan raft-associated proteolipid predominantly expressed by oligodendrocytes and Schwann cells. We show that genetic ablation of mal resulted in cytoplasmic inclusions within compact myelin, paranodal loops that are everted away from the axon, and disorganized transverse bands at the paranode--axon interface in the adult central nervous system. These structural changes were accompanied by a marked reduction of contactin-associated protein/paranodin, neurofascin 155 (NF155), and the potassium channel Kv1.2, whereas nodal clusters of sodium channels were unaltered. Initial formation of paranodal regions appeared normal, but abnormalities became detectable when MAL started to be expressed. Biochemical analysis revealed reduced myelin-associated glycoprotein, myelin basic protein, and NF155 protein levels in myelin and myelin-derived rafts. Our results demonstrate a critical role for MAL in the maintenance of central nervous system paranodes, likely by controlling the trafficking and/or sorting of NF155 and other membrane components in oligodendrocytes.

AB - The myelin and lymphocyte protein (MAL) is a tetraspan raft-associated proteolipid predominantly expressed by oligodendrocytes and Schwann cells. We show that genetic ablation of mal resulted in cytoplasmic inclusions within compact myelin, paranodal loops that are everted away from the axon, and disorganized transverse bands at the paranode--axon interface in the adult central nervous system. These structural changes were accompanied by a marked reduction of contactin-associated protein/paranodin, neurofascin 155 (NF155), and the potassium channel Kv1.2, whereas nodal clusters of sodium channels were unaltered. Initial formation of paranodal regions appeared normal, but abnormalities became detectable when MAL started to be expressed. Biochemical analysis revealed reduced myelin-associated glycoprotein, myelin basic protein, and NF155 protein levels in myelin and myelin-derived rafts. Our results demonstrate a critical role for MAL in the maintenance of central nervous system paranodes, likely by controlling the trafficking and/or sorting of NF155 and other membrane components in oligodendrocytes.

KW - Animals

KW - Axons

KW - Cell Adhesion Molecules

KW - Cell Communication

KW - Central Nervous System

KW - Down-Regulation

KW - Kv1.2 Potassium Channel

KW - Membrane Microdomains

KW - Membrane Transport Proteins

KW - Mice

KW - Mice, Knockout

KW - Microscopy, Electron

KW - Myelin Basic Protein

KW - Myelin Proteins

KW - Myelin Sheath

KW - Myelin and Lymphocyte-Associated Proteolipid Proteins

KW - Myelin-Associated Glycoprotein

KW - Nerve Growth Factors

KW - Neural Conduction

KW - Oligodendroglia

KW - Optic Nerve

KW - Potassium Channels

KW - Potassium Channels, Voltage-Gated

KW - Protein Transport

KW - Proteolipids

KW - Ranvier's Nodes

KW - Sciatic Nerve

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1083/jcb.200406092

DO - 10.1083/jcb.200406092

M3 - SCORING: Journal article

C2 - 15337780

VL - 166

SP - 731

EP - 742

JO - J CELL BIOL

JF - J CELL BIOL

SN - 0021-9525

IS - 5

ER -