HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 282, Issue 32, 23491-23499, August 10, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/32/23491    most recent M611703200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal 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 Google Scholar Google Scholar Articles by Konishi, H. Articles by Kiyama, H. Search for Related Content PubMed PubMed Citation Articles by Konishi, H. Articles by Kiyama, H. Social Bookmarking                      What's this?

Identification of Peripherin as a Akt Substrate in Neurons^*

Hiroyuki Konishi, Kazuhiko Namikawa, Keiji Shikata^¶, Yuji Kobatake, Taro Tachibana^¶, and Hiroshi Kiyama¹

From the Department of Anatomy and Neurobiology, Osaka City University, Graduate School of Medicine, Osaka 545-8585, Japan, the Department of Anatomy, Asahikawa Medical College, Asahikawa, Hokkaido 078-8510, Japan, and the ^¶Department of Bioengineering, Osaka City University, Graduate School of Engineering, Osaka 558-8585, Japan

Activation of Akt-mediated signaling pathways is crucial for survival and regeneration of injured neurons. In this study, we attempted to identify novel Akt substrates by using an antibody that recognized a consensus motif phosphorylated by Akt. PC12 cells that overexpressed constitutively active Akt were used. Using two-dimensional PAGE, we identified protein spots that exhibited increased immunostaining of the antibody. Mass spectrometry revealed several major spots as the neuronal intermediate filament protein, peripherin. Using several peripherin fragments, the phosphorylation site was determined as Ser⁶⁶ in its head domain in vitro. Furthermore, a co-immunoprecipitation experiment revealed that Akt interacted with the head domain of peripherin in HEK 293T cells. An antibody against phosphorylated peripherin was raised, and induction of phosphorylated peripherin was observed not only in Akt-activated cultured cells but also in nerve-injured hypoglossal motor neurons. These results suggest that peripherin is a novel substrate for Akt in vivo and that its phosphorylation may play a role in motor nerve regeneration.

Received for publication, December 21, 2006 , and in revised form, May 22, 2007.

^* This work was supported in part by grants from the Ministry of Health, Labor and Welfare of Japan, the Ministry of Education, Culture, Sports, Science, and Technology, and the General Insurance Association of Japan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Dept. of Anatomy and Neurobiology, Osaka City University, Graduate School of Medicine, 1-4-3 Abeno-ku, Asahimachi, Osaka 545-8585, Japan. Tel.: 81-6-6645-3701; Fax: 81-6-6645-3702; E-mail: kiyama{at}med.osaka-cu.ac.jp.

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

This article has been cited by other articles:

				D. Diez, C. Grijota-Martinez, P. Agretti, G. De Marco, M. Tonacchera, A. Pinchera, G. Morreale de Escobar, J. Bernal, and B. Morte Thyroid Hormone Action in the Adult Brain: Gene Expression Profiling of the Effects of Single and Multiple Doses of Triiodo-L-Thyronine in the Rat Striatum Endocrinology, August 1, 2008; 149(8): 3989 - 4000. [Abstract] [Full Text] [PDF]