English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Sox10 cooperates with the mediator subunit 12 during terminal differentiation of myelinating glia

Vogl, M. R., Reiprich, S., Küspert, M., Kosian, T., Schrewe, H., Nave, K.-A., et al. (2013). Sox10 cooperates with the mediator subunit 12 during terminal differentiation of myelinating glia. The Journal of Neuroscience: the Official Journal of the Society for Neuroscience, 33(15), 6679-6690. doi:10.1523/JNEUROSCI.5178-12.2013.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-9314-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-9315-E
Genre: Journal Article

Files

show Files
hide Files
:
Vogl.pdf (Publisher version), 3MB
Name:
Vogl.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
© 2013 the authors
License:
-

Locators

show

Creators

show
hide
 Creators:
Vogl, Michael R. , Author
Reiprich, Simone , Author
Küspert, Melanie , Author
Kosian, Thomas, Author
Schrewe, Heinrich1, Author              
Nave, Klaus-Armin , Author
Wegner, Michael , Author
Affiliations:
1Dept. of Developmental Genetics (Head: Bernhard G. Herrmann), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433548              

Content

show
hide
Free keywords: -
 Abstract: Several transcription factors are essential for terminal differentiation of myelinating glia, among them the high-mobility-group-domain-containing protein Sox10. To better understand how these factors exert their effects and shape glial expression programs, we identified and characterized a physical and functional link between Sox10 and the Med12 subunit of the Mediator complex that serves as a conserved multiprotein interphase between transcription factors and the general transcription machinery. We found that Sox10 bound with two of its conserved domains to the C-terminal region of Med12 and its close relative, Med12-like. In contrast to Med12-like, substantial amounts of Med12 were detected in both Schwann cells and oligodendrocytes. Its conditional glia-specific deletion in mice led to terminal differentiation defects that were highly reminiscent of those obtained after Sox10 deletion. In support of a functional cooperation, both proteins were jointly required for Krox20 induction and were physically associated with the critical regulatory region of the Krox20 gene in myelinating Schwann cells. We conclude that Sox10 functions during terminal differentiation of myelinating glia, at least in part by Med12-dependent recruitment of the Mediator complex.

Details

show
hide
Language(s): eng - English
 Dates: 2013-04-10
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1523/JNEUROSCI.5178-12.2013
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: The Journal of Neuroscience : the Official Journal of the Society for Neuroscience
  Other : J. Neurosci.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Baltimore, MD : The Society
Pages: - Volume / Issue: 33 (15) Sequence Number: - Start / End Page: 6679 - 6690 Identifier: ISSN: 0270-6474
CoNE: https://pure.mpg.de/cone/journals/resource/954925502187_1