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Nat. Cell Biol. Jan (2002); 4(1):73-8
The exocyst complex binds the small GTPase RalA to mediate filopodia formation.
Sugihara K, Asano S, Tanaka K, Iwamatsu A, Okawa K, Ohta Y
Hematology Division, Department of Medicine, Brigham and women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
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.
[PUBMED: 11744922] Download Biogrid Interactions in a variety of formats including PSI FormatPUBMED
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Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.