JCB logo
MBoC5 from Garland Science
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online October 6, 2008
doi:10.1083/jcb.200807052
The Journal of Cell Biology, Vol. 183, No. 1, 11-17
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Jang et al.
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 4087K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Google Scholar
Right arrow Articles by Jang, C.
Right arrow Articles by Chung, J.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jang, C.
Right arrow Articles by Chung, J.
Related Collections
Right arrowRelated Article
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Report

 LKB1 induces apical trafficking of Silnoon, a monocarboxylate transporter, in Drosophila melanogaster

Cholsoon Jang1,2, Gina Lee1,2, and Jongkyeong Chung1,2

1 National Creative Research Initiatives Center for Cell Growth Regulation and 2 Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Yusong-gu, Taejon 305-701, Korea

Correspondence to Jongkyeong Chung: jchung{at}kaist.ac.kr

Silnoon (Sln) is a monocarboxylate transporter (MCT) that mediates active transport of metabolic monocarboxylates such as butyrate and lactate. Here, we identify Sln as a novel LKB1-interacting protein using Drosophila melanogaster genetic modifier screening. Sln expression does not affect cell cycle progression or cell size but specifically enhances LKB1-dependent apoptosis and tissue size reduction. Conversely, down-regulation of Sln suppresses LKB1-dependent apoptosis, implicating Sln as a downstream mediator of LKB1. The kinase activity of LKB1 induces apical trafficking of Sln in polarized cells, and LKB1-dependent Sln trafficking is crucial for triggering apoptosis induced by extracellular butyrate. Given that LKB1 functions to control both epithelial polarity and cell death, we propose Sln is an important downstream target of LKB1.

Abbreviations used in this paper: AMPK, AMP-activated protein kinase; AO, acridine orange; MCT, monocarboxylate transporter; rp49, ribosomal protein 49; Sln, Silnoon.

© 2008 Jang et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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

Related Article

Novel role for the LKB1 pathway in controlling monocarboxylate fuel transporters
Beatrice Maria Filippi and Dario R. Alessi
J. Cell Biol. 2008 183: 7-9. [Abstract] [Full Text] [PDF]



This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents