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J. Biol. Chem., Vol. 282, Issue 39, 28939-28950, September 28, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/39/28939    most recent M700283200v1 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 Shin, N. Articles by Chang, S. Search for Related Content PubMed PubMed Citation Articles by Shin, N. Articles by Chang, S. Social Bookmarking                      What's this?

Sorting Nexin 9 Interacts with Dynamin 1 and N-WASP and Coordinates Synaptic Vesicle Endocytosis^*

Narae Shin, Suho Lee, Namhui Ahn, Soo-A Kim, Sang-Gun Ahn^¶, Zee YongPark, and Sunghoe Chang¹

From the Department of Life Science, Gwangju Institute of Science and Technology, Gwangju 500-712, the Department of Biochemistry, Dongguk University, College of Oriental Medicine, Gyeongju 780-714, and the ^¶Department of Pathology, Chosun University, College of Dentistry, Gwangju 501-759, South Korea

Sorting nexin 9 (SNX9) is a member of the sorting nexin family of proteins, each of which contains a characteristic Phox homology domain. SNX9 is widely expressed and plays a role in clathrin-mediated endocytosis, but it is not known if it is present in neuronal cells. We report that SNX9 is expressed in the presynaptic compartment of cultured hippocampal neurons, where it binds to dynamin-1 and N-WASP. Overexpression of full-length SNX9 or a C-terminal truncated version caused severe defects in synaptic vesicle endocytosis during, as well as after, stimulation. Knockdown of SNX9 with short interfering RNA also reduced synaptic vesicle endocytosis, and the W39A mutation of SNX9 abolished the inhibitory effect of SNX9 on endocytosis. Rescue experiments showed that most of the effect of SNX9 on endocytosis results from its interaction with dynamin 1, although its interaction with N-WASP contributes in some degree. We further showed that SNX9 dimerizes through its C-terminal domain, suggesting that it may interact simultaneously with dynamin 1 and N-WASP. We propose that SNX9 interacts with dynamin-1 and N-WASP in presynaptic terminals, where it links actin dynamics and synaptic vesicle endocytosis.

Received for publication, January 10, 2007 , and in revised form, July 25, 2007.

^* This work was supported by Grant M103KV010009-06K2201-00910 from the Brain Research Center of the 21st Century Frontier Research Program (to S. C.), by the Ministry of Science and Technology, and by Grant KRF-2006-C00515 from the Korea Research Foundation (to S. C.) funded by the Korean Government (MOEHRD, Basic Research Promotion Fund), the Republic of Korea. 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 Life Science, Gwangju Institute of Science and Technology, 1 Oryong-dong Buk-gu, Gwangju, South Korea. Tel.: 82-62-970-2495; Fax: 82-62-970-2484; E-mail: sunghoe{at}gist.ac.kr.

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