MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Friedrich, R. P.
Right arrow Articles by Wegner, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Friedrich, R. P.
Right arrow Articles by Wegner, M.
Molecular and Cellular Biology, March 2005, p. 1821-1829, Vol. 25, No. 5
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.5.1821-1829.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The Class III POU Domain Protein Brn-1 Can Fully Replace the Related Oct-6 during Schwann Cell Development and Myelination

Ralf P. Friedrich,1,{dagger} Beate Schlierf,1,{dagger} Ernst R. Tamm,2 Michael R. Bösl,3 and Michael Wegner1*

Institut für Biochemie,1 Institut für Anatomie, Universität Erlangen-Nürnberg, Erlangen,2 Max-Planck-Institut für Neurobiologie, Martinsried, Germany3

Received 29 July 2004/ Accepted 20 November 2004

For differentiation, Schwann cells rely on the class III POU domain transcription factor Oct-6, which is expressed transiently when Schwann cells have established a one-to-one relation with axons but have not yet started to myelinate. Loss of Oct-6 leads to a transient arrest in this promyelinating stage and a delay in myelination. Although the closely related POU domain protein Brn-2 is coexpressed with Oct-6 in Schwann cells, its loss has only mild consequences. Combined loss of both POU domain proteins, in contrast, dramatically increases the myelination delay, raising the question of how related POU domain proteins compare to each other in their activities. Here, we have replaced Oct-6 expression in the mouse with expression of the class III POU domain protein Brn-1. Although this protein is not normally expressed in Schwann cells, Brn-1 was capable of fully replacing Oct-6. Brn-1 efficiently induced Krox-20 expression as a prerequisite for myelination. Onset and extent of myelination were also indistinguishable from that of the wild type in mice that carried only Brn-1 instead of Oct-6 alleles. Similar to Oct-6, Brn-1 down-regulated its own expression at later stages of myelination. Thus, class III POU domain proteins can fully replace each other in Schwann cell development.


* Corresponding author. Mailing address: Institut für Biochemie, Universität Erlangen, Fahrstrasse 17, 91054 Erlangen, Germany. Phone: 49-(0)9131-85-24620. Fax: 49-(0)9131-85-22484. E-mail: m.wegner{at}biochem.uni-erlangen.de.

{dagger} R.P.F. and B.S. contributed equally.


Molecular and Cellular Biology, March 2005, p. 1821-1829, Vol. 25, No. 5
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.5.1821-1829.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2005 by the American Society for Microbiology. All rights reserved.