GTC
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Genes to Cells (2005) 10, 465-476. doi:10.1111/j.1365-2443.2005.00848.x
© 2005 Blackwell Publishing or its licensors

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
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 Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yoshida, K.
Right arrow Articles by Shirataki, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yoshida, K.
Right arrow Articles by Shirataki, H.

Interaction of the taxilin family with the nascent polypeptide-associated complex that is involved in the transcriptional and translational processes

Kenji Yoshida1,2, Satoru Nogami1, Sachie Satoh1, Sawako Tanaka-Nakadate1, Hideyuki Hiraishi2, Akira Terano2 and Hiromichi Shirataki1,*

1 Division of Molecular and Cell Biology, Institute for Medical Science
2 Department of Gastroenterology, Dokkyo University School of Medicine, 880 Kitakobayashi, Mibu-machi, Tochigi 321-0293, Japan

{alpha}-Taxilin is a novel binding partner of the syntaxin family, which is implicated in intracellular vesicle traffic. We have here found that {alpha}-taxilin interacts with the nascent polypeptide-associated complex (NAC), which is involved in transferring growing nascent polypeptide chains to appropriate co-translationally acting factors. NAC is composed of two subunits, {alpha}- and ßNACs. Both these subunits bound to {alpha}-taxilin through its C-terminal coiled-coil region in dose-dependent and saturable manners. The interactions of {alpha}-taxilin with {alpha}NAC and NAC but not with ßNAC were inhibited by syntaxin-4, indicating that {alpha}-taxilin binds to NAC mainly through its interaction with {alpha}NAC. When {alpha}NAC was over-expressed in COS-7 cells, {alpha}NAC was distributed in the cytosol and nucleus. However, co-expression of the {alpha}-taxilin fragment containing the {alpha}NAC-binding region eliminated the nuclear distribution of over-expressed {alpha}NAC. Moreover, other taxilin family members, ß- and {gamma}-taxilins, also bound to {alpha}NAC and thereby affected the nuclear distribution of over-expressed {alpha}NAC. Taken together with the evidence that {alpha}NAC functions in the nucleus as a transcriptional coactivator, our results raise the possibility that the taxilin family is involved not only in the translational process through its interaction with NAC but also in the transcriptional process through its interaction with {alpha}NAC alone.


Communicated by: Yoshimi Takai

* Correspondence: E-mail: hiro-sh{at}dokkyomed.ac.jp




This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
O. Panasenko, E. Landrieux, M. Feuermann, A. Finka, N. Paquet, and M. A. Collart
The Yeast Ccr4-Not Complex Controls Ubiquitination of the Nascent-associated Polypeptide (NAC-EGD) Complex
J. Biol. Chem., October 20, 2006; 281(42): 31389 - 31398.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS
Copyright © 2005 by Wiley-Blackwell Publishing.