JCB logo
PeproTech: Your source for Cell Biology Research Reagents
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 1 August 2005. doi:10.1083/jcb.200501138
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 170, Number 3, 401-411
This Article
Right arrow Full Text
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Besirli, C. G.
Right arrow Articles by Johnson, E. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Besirli, C. G.
Right arrow Articles by Johnson, E. M., Jr.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Article

 The limited role of NH2-terminal c-Jun phosphorylation in neuronal apoptosis : Identification of the nuclear pore complex as a potential target of the JNK pathway



Cagri G. Besirli1, Erwin F. Wagner2, and Eugene M. Johnson, Jr.1,2

1 Departments of Neurology and Molecular Biology & Pharmacology, Washington University School of Medicine, St. Louis, MO 63110
2 Research Institute of Molecular Pathology (IMP), 1030 Vienna, Austria

Correspondence to Eugene M. Johnson Jr.: eugene.johnson{at}wustl.edu

c-Jun is induced in many neuronal death paradigms. A critical step in c-Jun regulation involves phosphorylation of Ser63/Ser73 located in the NH2-terminal transactivation domain. To determine the importance of this phosphorylation for neuronal apoptosis, we analyzed the sympathetic neurons of mice carrying a mutant c-Jun gene that lacks Ser63/Ser73 phosphorylation sites (jun aa). Trophic factor–deprivation or DNA damage–induced death was significantly delayed in jun aa/aa neurons. Neuronal c-Jun induction was only partially inhibited, demonstrating that phosphorylation of Ser63/73 is not required for c-Jun activation. The inductions of proapoptotic BH3-only proteins, Bim and PUMA/Bbc3, were delayed during neuronal apoptosis in mutant neurons. These results demonstrate that NH2-terminal c-Jun phosphorylation is important, but not necessary, for the induction of proapoptotic genes and neuronal apoptosis. Thus, additional JNK substrates may be critical for neuronal death. As potential mediators, we identified additional nuclear MLK/JNK substrates, including Nup214 subunit of the nuclear pore complex.

Abbreviations used: DIV, days in vitro; JNK, Jun–NH2-terminal kinase; MLK, mixed lineage kinase; NPC, nuclear pore complex; Nup, nucleoporin; P, postnatal day; SCG, superior cervical ganglion.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents