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

HOME  |   SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

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 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 Web of Science (10) Citing Articles via Google Scholar Google Scholar Articles by Lu, D. Articles by Raizada, M. K. Search for Related Content PubMed PubMed Citation Articles by Lu, D. Articles by Raizada, M. K. Pubmed/NCBI databases Compound via MeSH Substance via MeSH

 Previous Article  |  Next Article 

The Journal of Neuroscience, February 15, 1998, 18(4):1329-1336

Involvement of p62 Nucleoporin in Angiotensin II-Induced Nuclear Translocation of STAT3 in Brain Neurons

Di Lu, Hong Yang and Mohan K. Raizada

Department of Physiology, College of Medicine, University of Florida, Gainesville, Florida 32610

Chronic stimulation of brain neurons by angiotensin II (Ang II) results in a increase in norepinephrine (NE) uptake. This involves stimulation of transcription of NE transporter and tyrosine hydroxylase genes and is associated with translocation of signaling molecules and transcription factors from the cytoplasmic compartment into the neuronal nucleus (). We report here that the phosphorylation of p62, a glycoprotein nucleoporin of the nuclear pore complex (NPC), by MAP kinase is involved in this process. Ang II caused a time-dependent translocation of signal transducers and activators of transcription (STAT3) from the cytoplasmic compartment into the nucleus. This translocation was attenuated by pretreatment with antisense oligonucleotide (AON) to MAP kinase. Ang II also stimulated phosphorylation of p62, and a maximal phosphorylation of 12-fold was observed with 100 nM Ang II. This stimulation was blocked by losartan, an AT₁ receptor subtype-specific antagonist. The conclusion that MAP kinase is involved in Ang II-induced phosphorylation of p62 and nuclear translocation of STAT3 is supported by the following. (1) p62 phosphorylation was blocked by a peptide that competes with p62 as a MAP kinase substrate both in vitro and in vivo; (2) AON to MAP kinase attenuated Ang II stimulation of p62 phosphorylation; and (3) in addition, it also blocked nuclear translocation of STAT3. Intracellular loading of the peptide containing MAP kinase substrate consensus of the p62 reduced Ang II stimulation of p62 phosphorylation and nuclear translocation of STAT3 in both in vivo and in vitro experiments. These observations suggest that Ang II-induced phosphorylation of p62 may accelerate the activity of the NPC, which would result in an increase in the nuclear transport of transcription factors and signaling molecules. This will stimulate transcriptional processes associated with Ang II regulation of NE neuromodulation.

Key words: angiotensin; MAP kinase; nuclear translocation; signal transduction; p62; nuclear pore complex

---

Copyright © 1998 Society for Neuroscience  0270-6474/98/1841329-08$05.00/0

This article has been cited by other articles:

				M. V. Bardina, P. V. Lidsky, E. V. Sheval, K. V. Fominykh, F. J. M. van Kuppeveld, V. Y. Polyakov, and V. I. Agol Mengovirus-Induced Rearrangement of the Nuclear Pore Complex: Hijacking Cellular Phosphorylation Machinery J. Virol., April 1, 2009; 83(7): 3150 - 3161. [Abstract] [Full Text] [PDF]

				K. D. Pendergrass, D. B. Averill, C. M. Ferrario, D. I. Diz, and M. C. Chappell Differential expression of nuclear AT1 receptors and angiotensin II within the kidney of the male congenic mRen2.Lewis rat Am J Physiol Renal Physiol, June 1, 2006; 290(6): F1497 - F1506. [Abstract] [Full Text] [PDF]

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help