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Functionally distinct PI 3-kinase pathways regulate myelination in the peripheral nervous system.

Bradley A Heller1, Monica Ghidinelli, Jakob Voelkl

  • 1Neuroscience Institute and 2 Departments of Neuroscience and Physiology and Neurology, NYU Langone Medical Center, New York, NY 10016.

The Journal of Cell Biology
|April 2, 2014
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The PI 3-kinase (PI 3-K) pathway has distinct roles in Schwann cell myelination. One pathway promotes myelination early on, while another later pathway negatively regulates it.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • The Phosphoinositide 3-kinase (PI 3-K) signaling pathway is crucial for Schwann cell myelination.
  • Understanding the specific effectors and their roles in myelination is essential for comprehending peripheral nerve development.

Purpose of the Study:

  • To characterize PI 3-K pathway effectors activated during Schwann cell myelination.
  • To elucidate the distinct roles of identified effectors in regulating myelination processes.

Main Methods:

  • Probing myelinating cultures and developing nerves with antibodies recognizing phosphorylated PI 3-K substrates.
  • Analyzing the expression patterns of key proteins like S6 ribosomal protein (S6rp) and N-myc downstream-regulated gene-1 (NDRG1).
  • Investigating the roles of Neuregulin1, laminin-2, α6β4 integrin, and Sgk1 in PI 3-K signaling during myelination.

Main Results:

  • Identified S6rp as a down-regulated phospho-protein at myelination onset and NDRG1 as a strikingly up-regulated phospho-protein.
  • Type III Neuregulin1 activates S6rp (mTORC1 effector) on the axon.
  • Laminin-2, via α6β4 integrin and Sgk1, drives NDRG1 phosphorylation in Cajal bands.
  • Mice lacking α6β4 integrin or Sgk1 signaling show hypermyelination.

Conclusions:

  • PI 3-K signaling involves spatially and functionally distinct pathways in myelination.
  • An early, pro-myelinating pathway is driven by axonal Neuregulin1.
  • A later pathway, dependent on laminin-integrin signaling, negatively regulates myelination.