Skip Navigation

This Article
Right arrow Print PDF (1643K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (20)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Bannister, A.J.
Right arrow Articles by Kouzarides, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bannister, A.J.
Right arrow Articles by Kouzarides, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1994, Vol. 22, No. 24 5173-5176
© 1994

Articles

Phosphorylation of the c-Fos and c-Jun HOB1 motif stimulates its activation capacity

A.J. Bannister, H.J. Brown, J.A. Sutherland and T. Kouzarides*

Wellcome/CRC Institute, Tennis Court Road Cambridge CB2 1QR Department of Pathology, University of Cambridge Cambridge, UK

*To whom correspondence should be addressed

Received October 14, 1994. Accepted November 8, 1994.

The c-Fos and c-Jun proteins bind an AP1 site and activate transcription synerglstically. These two proteins have a common activation domain which has two co-operating motifs, HOB1 and HOB2. The HOB1 motif of c-Jun includes S73 which Is required for Ha-Ras-lnduced super-activation and phosphorylation by MAP kinase-like enzymes. Since c-Fos H0B1 has a conserved Thr residue (T232) analogous to c-Jun S73 we have proposed that c-Fos HOB1 will be regulated In the same way as c-Jun HOB1. Here we show that the HOB1-containing activation domain of c-Fos Is stimulated by Ha-Ras In vivo and phosphorylated by a MAP klnase family member In vitro and that mutating T232 to Ala abolishes both functions. Collectively these results suggest that phosphorylation of the HOB1 motif Increases its activation capacity. To provide direct evidence for this we change the context of c-Fos T232 to a PKA recognition site, and show that HOB1 activity Is now stimulated by the catalytic subunit of PKA. This 'PKA specificity' experiment represents a novel and powerful way to analyse phosphorylation events involved in a variety of biological functions.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 EndocrinologyHome page
M. C. Opazo, A. Gianini, F. Pancetti, G. Azkcona, L. Alarcon, R. Lizana, V. Noches, P. A. Gonzalez, M. Porto, S. Mora, et al.
Maternal Hypothyroxinemia Impairs Spatial Learning and Synaptic Nature and Function in the Offspring
Endocrinology, October 1, 2008; 149(10): 5097 - 5106.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
G. Bossis, C. E. Malnou, R. Farras, E. Andermarcher, R. Hipskind, M. Rodriguez, D. Schmidt, S. Muller, I. Jariel-Encontre, and M. Piechaczyk
Down-Regulation of c-Fos/c-Jun AP-1 Dimer Activity by Sumoylation
Mol. Cell. Biol., August 15, 2005; 25(16): 6964 - 6979.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
P. Monje, M. J. Marinissen, and J. S. Gutkind
Phosphorylation of the Carboxyl-Terminal Transactivation Domain of c-Fos by Extracellular Signal-Regulated Kinase Mediates the Transcriptional Activation of AP-1 and Cellular Transformation Induced by Platelet-Derived Growth Factor
Mol. Cell. Biol., October 1, 2003; 23(19): 7030 - 7043.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
R. C. Elliott and C. M. Gall
Changes in Activating Protein 1 (AP-1) Composition Correspond with the Biphasic Profile of Nerve Growth Factor mRNA Expression in Rat Hippocampus after Hilus Lesion-Induced Seizures
J. Neurosci., March 15, 2000; 20(6): 2142 - 2149.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.