The exocyst complex binds the small GTPase RalA to mediate filopodia formation

Kazuhiro Sugihara; Shiro Asano; Kenichi Tanaka; Akihiro Iwamatsu; Katsuya Okawa; Yasutaka Ohta

doi:10.1038/ncb720

The exocyst complex binds the small GTPase RalA to mediate filopodia formation

Kazuhiro Sugihara, Shiro Asano, Kenichi Tanaka, Akihiro Iwamatsu, Katsuya Okawa, Yasutaka Ohta

Research output: Contribution to journal › Article › peer-review

209 Citations (Scopus)

Abstract

The Ras-related small GTPase RalA is involved in controlling actin cytoskeletal remodelling and vesicle transport in mammalian cells^{1, 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-α (TNF-α) 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.

Original language	English
Pages (from-to)	73-78
Number of pages	6
Journal	Nature Cell Biology
Volume	4
Issue number	1
DOIs	https://doi.org/10.1038/ncb720
Publication status	Published - 2002
Externally published	Yes

All Science Journal Classification (ASJC) codes

Cell Biology

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10.1038/ncb720

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title = "The exocyst complex binds the small GTPase RalA to mediate filopodia formation",

abstract = "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-α (TNF-α) 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.",

author = "Kazuhiro Sugihara and Shiro Asano and Kenichi Tanaka and Akihiro Iwamatsu and Katsuya Okawa and Yasutaka Ohta",

note = "Funding Information: ACKNOWLEDGEMENTS We thank T. Stossel and J. Hartwig for critical reading of the manuscript. This work was supported by Grant HL19429 from the United States Public Health Service and by the Edwin S. Webster Foundation. Correspondence and requests for material should be addressed to Y.O. Supplementary information is available on Nature Cell Biology{\textquoteright}s website (http://cellbio.nature.com/).",

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doi = "10.1038/ncb720",

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T1 - The exocyst complex binds the small GTPase RalA to mediate filopodia formation

AU - Sugihara, Kazuhiro

AU - Asano, Shiro

AU - Tanaka, Kenichi

AU - Iwamatsu, Akihiro

AU - Okawa, Katsuya

AU - Ohta, Yasutaka

N1 - Funding Information: ACKNOWLEDGEMENTS We thank T. Stossel and J. Hartwig for critical reading of the manuscript. This work was supported by Grant HL19429 from the United States Public Health Service and by the Edwin S. Webster Foundation. Correspondence and requests for material should be addressed to Y.O. Supplementary information is available on Nature Cell Biology’s website (http://cellbio.nature.com/).

PY - 2002

Y1 - 2002

N2 - 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-α (TNF-α) 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.

AB - 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-α (TNF-α) 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.

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The exocyst complex binds the small GTPase RalA to mediate filopodia formation

Abstract

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