Polarization and Myelination in Myelinating Glia

Masaki, Toshihiro

doi:10.5402/2012/769412

Cited by 19 publications

(16 citation statements)

References 352 publications

(455 reference statements)

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“…Lipid rafts are characterized by the concentration of selected membrane lipids such as cholesterols, galactosylceramide, and low levels of phosphatidylcholine. These lipids have roles in myelin formation and stabilization [14,15] by including and excluding specific proteins into particular compartments and orchestrating membrane protein trafficking [16,17] and subsequent signal transduction [18] (see [16,19] for review). In CNS and PNS myelin, lipid rafts have been suggested to promote cellular adhesion by facilitating the localization of membrane and transmembrane proteins mediating axon-glia recognition [14,[20][21][22][23][24].…”

Section: Myelin Lipids-role Of Lipids In Myelinmentioning

confidence: 99%

Myelin Fat Facts: An Overview of Lipids and Fatty Acid Metabolism

Poitelon

Kopec

Belin

2020

Cells

250

152

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Myelin is critical for the proper function of the nervous system and one of the most complex cell–cell interactions of the body. Myelination allows for the rapid conduction of action potentials along axonal fibers and provides physical and trophic support to neurons. Myelin contains a high content of lipids, and the formation of the myelin sheath requires high levels of fatty acid and lipid synthesis, together with uptake of extracellular fatty acids. Recent studies have further advanced our understanding of the metabolism and functions of myelin fatty acids and lipids. In this review, we present an overview of the basic biology of myelin lipids and recent insights on the regulation of fatty acid metabolism and functions in myelinating cells. In addition, this review may serve to provide a foundation for future research characterizing the role of fatty acids and lipids in myelin biology and metabolic disorders affecting the central and peripheral nervous system.

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Section: Myelin Lipids-role Of Lipids In Myelinmentioning

confidence: 99%

Myelin Fat Facts: An Overview of Lipids and Fatty Acid Metabolism

Poitelon

Kopec

Belin

2020

Cells

250

152

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“…In generating a myelin membrane, OLGs acquire a polarized phenotype. The sphingolipidenriched myelin membrane is served by a basolateral-surface-like mechanism, while the cell body plasma membrane is served by an apical-surface-like transport mechanism (4)(5)(6)(7)(8). MBP and PLP stabilize apposed myelin membrane surfaces in compact myelin, and their transport routes are segregated.…”

mentioning

confidence: 99%

The Major Myelin-Resident Protein PLP Is Transported to Myelin Membranes via a Transcytotic Mechanism: Involvement of Sulfatide

Baron

Ozgen

Klunder

et al. 2015

Molecular and Cellular Biology

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bMyelin membranes are sheet-like extensions of oligodendrocytes that can be considered membrane domains distinct from the cell's plasma membrane. Consistent with the polarized nature of oligodendrocytes, we demonstrate that transcytotic transport of the major myelin-resident protein proteolipid protein (PLP) is a key element in the mechanism of myelin assembly. Upon biosynthesis, PLP traffics to myelin membranes via syntaxin 3-mediated docking at the apical-surface-like cell body plasma membrane, which is followed by subsequent internalization and transport to the basolateral-surface-like myelin sheet. Pulse-chase experiments, in conjunction with surface biotinylation and organelle fractionation, reveal that following biosynthesis, PLP is transported to the cell body surface in Triton X-100 (TX-100)-resistant microdomains. At the plasma membrane, PLP transiently resides within these microdomains and its lateral dissipation is followed by segregation into 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS)-resistant domains, internalization, and subsequent transport toward the myelin membrane. Sulfatide triggers PLP's reallocation from TX-100-into CHAPS-resistant membrane domains, while inhibition of sulfatide biosynthesis inhibits transcytotic PLP transport. Taking these findings together, we propose a model in which PLP transport to the myelin membrane proceeds via a transcytotic mechanism mediated by sulfatide and characterized by a conformational alteration and dynamic, i.e., transient, partitioning of PLP into distinct membrane microdomains involved in biosynthetic and transcytotic transport.

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“…Schwann cells are highly polarized cells with both longitudinal and radial axes of polarity (Masaki, ; Pereira, Lebrun‐Julien, & Suter, ; Salzer, ). This polarity is essential for proper myelination and the fidelity of domain formation, including the organization of the underlying axon (Zollinger, Baalman, & Rasband, ).…”

Section: Discussionmentioning

confidence: 99%

Necl‐4/Cadm4 recruits Par‐3 to the Schwann cell adaxonal membrane

Meng

Maurel

Lam

et al. 2018

Glia

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Interactions between axons and Schwann cells are essential for the acquisition of Schwann cell radial and longitudinal polarity and myelin sheath assembly. In the internode, the largest of these longitudinal domains, axon-Schwann cell interactions are mediated by the Nectin-like (Necl) cell adhesion proteins, also known as SynCAMs or Cadms. In particular, Necl-1/Cadm3 expressed on the axon surface binds to Necl-4/Cadm4 expressed along the adaxonal membrane of myelinating Schwann cells. Necl-4 promotes myelination in vitro and is required for the timely onset of myelination and the fidelity of the organization of the myelin sheath and the internode in vivo. A key question is the identity of the downstream effectors of Necl-4 that mediate its effects. The cytoplasmic terminal region (CTR) of Necl-4 contains a PDZ-domain binding motif. Accordingly, we used the CTR of Necl-4 in an unbiased proteomic screen of PDZ-domain proteins. We identify Par-3, a multi-PDZ domain containing protein of the Par-aPKC polarity complex previously implicated in myelination, as an interacting protein. Necl-4 and Par-3 are colocalized along the inner Schwann cell membrane and coprecipitate from Schwann cell lysates. The CTR of Necl-4 binds to the first PDZ domain of Par-3 thereby recruiting Par-3 to sites of Necl-4/Necl-1 interaction. Knockdown of Necl-4 perturbs Par-3 localization to the inner membrane of Schwann cells in myelinating co-cultures. These findings implicate interactions of Necl-1/Necl-4 in the recruitment of Par-3 to the Schwann cell adaxonal membrane and the establishment of Schwann cell radial polarity. K E Y W O R D S axon, cell adhesion, myelin, polarity, Schwann cell

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Polarization and Myelination in Myelinating Glia

Cited by 19 publications

References 352 publications

Myelin Fat Facts: An Overview of Lipids and Fatty Acid Metabolism

Myelin Fat Facts: An Overview of Lipids and Fatty Acid Metabolism

The Major Myelin-Resident Protein PLP Is Transported to Myelin Membranes via a Transcytotic Mechanism: Involvement of Sulfatide

Necl‐4/Cadm4 recruits Par‐3 to the Schwann cell adaxonal membrane

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