Brief Communication abstract
Nature Cell Biology 4, 73 - 78 (2001)
Published online: 17 December 2001 | doi:10.1038/ncb720
The exocyst complex binds the small GTPase RalA to mediate filopodia formation
Kazuhiro Sugihara1, Shiro Asano1, Kenichi Tanaka1, Akihiro Iwamatsu2, Katsuya Okawa2 & Yasutaka Ohta1
The Ras-related small GTPase RalA is involved in controlling actin cytoskeletal remodelling and vesicle transport in mammalian cells1, 2. We identified the mammalian homologue of Sec5, a subunit of the exocyst complex determining yeast cell polarity, as a specific binding partner for GTP-ligated RalA. Inhibition of RalA binding to Sec5 prevents filopod production by tumor necrosis factor-
(TNF-) and interleukin-1 (IL-1) and by activated forms of RalA and Cdc42, signalling intermediates downstream of these inflammatory cytokines. We propose that the RalA–exocyst complex interaction integrates the secretory and cytoskeletal pathways.
- Hematology Division, Department of Medicine, Brigham and women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA
- Section of Protein Chemistry, Central Laboratories for Key Technology, Kirin Brewery Company Ltd.,1-13-5 Fukuura, Kanazawa-ku, Yokohama-shi, Kanagawa 236-0004, Japan
Correspondence to: Yasutaka Ohta1 e-mail: yohta@rics.bwh.harvard.edu
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