Septin 7: Actin cross-organization is required for axonal association of Schwann cells

Myelin sheaths present two distinct domains: compacted myelin spirals and flanking non-compacted cytoplasmic channels, where lipid and protein segregation is established by unknown mechanisms. Septins, a conserved family of membrane and cytoskeletal interacting GTPases, form intracellular diffusion...

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Bibliographic Details
Main Authors: Alejandro D Roth, Dalinda Liazoghli, Felipe Perez De Arce, David R Colman
Format: Article
Language:English
Published: BMC 2013-01-01
Series:Biological Research
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Online Access:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602013000300004&lng=en&tlng=en
Description
Summary:Myelin sheaths present two distinct domains: compacted myelin spirals and flanking non-compacted cytoplasmic channels, where lipid and protein segregation is established by unknown mechanisms. Septins, a conserved family of membrane and cytoskeletal interacting GTPases, form intracellular diffusion barriers during cell division and neurite extension and are expressed in myelinating cells. Septins, particularly septin 7 (Sept7), the central constituent of septin polymers, are associated with the cytoplasmic channels of myelinating cells. Here we show that Schwann cells deprived of Sept7 fail to wrap around axons from dorsal root ganglion neurons and exhibit disorganization of the actin cytoskeleton. Likewise, Sept7 distribution is dependent on microfilament but not microtubule organization.
ISSN:0716-9760