spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

First published online April 3, 2008
doi: 10.1242/10.1242/jcs.016709

Journal of Cell Science 121, 1252-1263 (2008)
Published by The Company of Biologists 2008
This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
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
Right arrow reprints & permissions
Google Scholar
Right arrow Articles by Shin, N.
Right arrow Articles by Chang, S.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shin, N.
Right arrow Articles by Chang, S.

Research Article

SNX9 regulates tubular invagination of the plasma membrane through interaction with actin cytoskeleton and dynamin 2

Narae Shin1, Namhui Ahn1, Belle Chang-Ileto2, Joohyun Park1, Kohji Takei3, Sang-Gun Ahn4, Soo-A Kim5, Gilbert Di Paolo2 and Sunghoe Chang1,*

1 Department of Life Science, Gwangju Institute of Science and Technology, Gwangju 500-712, South Korea
2 Department of Pathology, College of Physicians and Surgeons, Columbia University Medical Center, New York, NY, USA
3 Department of Neuroscience, Okayama University, Okayamashi, Japan
4 Deparment of Pathology, Chosun University, Gwangju 501-759, South Korea
5 Department of Biochemistry, Dongguk University, Gyeongju 780-714, South Korea

* Author for correspondence (e-mail: sunghoe{at}gist.ac.kr)

Accepted 24 January 2008

Dynamic membrane remodeling during intracellular trafficking is controlled by the intricate interplay between lipids and proteins. BAR domains are modules that participate in endocytic processes by binding and deforming the lipid bilayer. Sorting nexin 9 (SNX9), which functions in clathrin-mediated endocytosis, contains a BAR domain, however, the properties of this domain are not well understood. Here we show that SNX9 shares many properties with other BAR domain-containing proteins, such as amphiphysin and endophilin. SNX9 is able to deform the plasma membrane, as well as liposomes, into narrow tubules and recruit N-WASP and dynamin 2 to these tubules via its SH3 domain. SNX9-induced tubulation is antagonized by N-WASP and dynamin 2 while it is enhanced by perturbation of actin dynamics. However, SNX9 also has several unique properties. The tubulating activity requires the BAR and PX domains, as well as the low-complexity (LC) domain, which binds the Arp2/3 complex. SNX9 also binds to PtdIns(4)P-5-kinases via its PX domain and its tubulating activity is regulated by phosphoinositides. In addition, the kinase activity of PtdIns(4)P-5-kinases is stimulated by interaction with SNX9, suggesting a positive feedback interaction between SNX9 and PtdIns(4)P-5-kinases. These results suggest that SNX9 functions in the coordination of membrane remodeling and fission via interactions with actin-regulating proteins, endocytic proteins and PtdIns(4,5)P2-metabolizing enzymes.

Key words: Sorting nexin 9 (SNX9), Bin-Amphiphysin-Rvs (BAR), Membrane tubulation, Clathrin-mediated endocytosis, Neural Wiskott-Aldrich syndrome protein (N-WASP), Dynamin, Actin cytoskeleton






© The Company of Biologists Ltd 2008