QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

HOME  |   SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

The Journal of Neuroscience, May 10, 2006, 26(19):5131-5142; doi:10.1523/JNEUROSCI.4970-05.2006

This Article Full Text Full Text (PDF) Submit an eLetter Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (14) Citing Articles via Google Scholar Google Scholar Articles by Ulery, P. G. Articles by Nestler, E. J. Search for Related Content PubMed PubMed Citation Articles by Ulery, P. G. Articles by Nestler, E. J.

 Previous Article  |  Next Article 

Cellular/Molecular
Regulation of FosB Stability by Phosphorylation

Paula G. Ulery,¹ Gabby Rudenko,² and Eric J. Nestler¹

¹Department of Psychiatry and Center for Basic Neuroscience, and ²Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390-9070

Correspondence should be addressed to Eric J. Nestler, 5323 Harry Hines Boulevard, Dallas, TX 75390-9070. Email: eric.nestler{at}utsouthwestern.edu

The transcription factor FosB (also referred to as FosB2 or FosB[short form]) is an important mediator of the long-term plasticity induced in brain by chronic exposure to several types of psychoactive stimuli, including drugs of abuse, stress, and electroconvulsive seizures. A distinct feature of FosB is that, once induced, it persists in brain for relatively long periods of time in the absence of further stimulation. The mechanisms underlying this apparent stability, however, have remained unknown. Here, we demonstrate that FosB is a relatively stable transcription factor, with a half-life of 10 h in cell culture. Furthermore, we show that FosB is a phosphoprotein in brain and that phosphorylation of a highly conserved serine residue (Ser27) in FosB protects it from proteasomal degradation. We provide several lines of evidence suggesting that this phosphorylation is mediated by casein kinase 2. These findings constitute the first evidence that FosB is phosphorylated and demonstrate that phosphorylation contributes to its stability, which is at the core of its ability to mediate long-lasting adaptations in brain.

Key words: FosB2; FosB; phosphorylation; casein kinase 2; protein stability; proteasomal degradation

---

Received Nov. 21, 2005; revised Feb. 21, 2006; accepted April 2, 2006.

Correspondence should be addressed to Eric J. Nestler, 5323 Harry Hines Boulevard, Dallas, TX 75390-9070. Email: eric.nestler{at}utsouthwestern.edu

This article has been cited by other articles:

				Y. Yan, K. Yamada, M. Niwa, T. Nagai, A. Nitta, and T. Nabeshima Enduring vulnerability to reinstatement of methamphetamine-seeking behavior in glial cell line-derived neurotrophic factor mutant mice FASEB J, July 1, 2007; 21(9): 1994 - 2004. [Abstract] [Full Text] [PDF]

				M. V. Karamouzis, P. A. Konstantinopoulos, and A. G. Papavassiliou The Activator Protein-1 Transcription Factor in Respiratory Epithelium Carcinogenesis Mol. Cancer Res., February 1, 2007; 5(2): 109 - 120. [Abstract] [Full Text] [PDF]

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help