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 cells. 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-alpha (TNF-alpha) 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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RalA binds directly to the exocyst members Sec5 and Exo84.
“RalA binds directly to the exocyst members Sec5 and Exo84”
From Ral mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst (2013) · cites this paper as Sugihara et al, 2002
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Abounit, S., & Zurzolo, C. (2012) · Journal of Cell Science · doi:10.1242/jcs.083279 · Cited by 386 · see citing works
Cryo-EM structure of the exocyst complex
Mei, K., Li, Y., Wang, S., Shao, G., Wang, J., Ding, Y., Luo, G., Yue, P., Liu, J.-J., Wang, X., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-017-0016-2 · Cited by 156 · see citing works
Systematic analysis of genome-wide fitness data in yeast reveals novel gene function and drug action
Hillenmeyer, M. E., Ericson, E., Davis, R. W., Nislow, C., Koller, D., & Giaever, G. (2010) · Genome Biology · doi:10.1186/gb-2010-11-3-r30 · Cited by 112 · see citing works
“The mammalian homolog is essential for development and participates in multiple biological processes, including vesicle targeting to the plasma membrane, protein translation, and filopodia extension [62,63].”
BackgroundRal mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst
Teodoro, R. O., Pekkurnaz, G., Nasser, A., Higashi‐Kovtun, M. E., Balakireva, M., McLachlan, I. G., Camonis, J., & Schwarz, T. L. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.147 · Cited by 61 · see citing works
- Authors
- Sugihara, K., Asano, S., Tanaka, K., Iwamatsu, A., Okawa, K., & Ohta, Y.
- Affiliations
- Brigham and Women's Hospital (US)
- Kirin (Japan) (JP)
- Corresponding author
- Ohta, Yasutaka
- Venue
- Nature Cell Biology
- Published
- 2001-12-17
- Volume
- 4
- Issue
- 1
- Pages
- 73-78
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2001717872
- Cited by
- 258
- References
- 0
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 4 · 2023: 1 · 2022: 2 · 2021: 5 · 2020: 3 · 2019: 8 · 2018: 9 · 2017: 9 · 2016: 7 · 2015: 9 · 2014: 11 · 2013: 13 · 2012: 19
- FWCI
- 5.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Edwin S. Webster Foundation
- National Heart, Lung, and Blood Institute (HL 19429)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- exocyst complex, RalA, Sec5, filopodia formation, small GTPases, actin cytoskeleton remodeling, vesicle trafficking, cell polarity, TNF-alpha signalling, IL-1 signaling, Cdc42, inflammatory cytokines, secretory pathway
- MeSH terms
- Animals, Binding Sites, Cytoskeleton, Exocytosis, Humans, Interleukin-1, Membrane Proteins, Protein Binding, Pseudopodia, Tumor Necrosis Factor-alpha, Signal Transduction, COS Cells, K562 Cells, GTP Phosphohydrolases, ral GTP-Binding Proteins, cdc42 GTP-Binding Protein, Vesicular Transport Proteins, Rats
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