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A 14-3-3γ dimer-based scaffold bridges CtBP1-S/BARS to PI(4)KIIIβ to regulate post-Golgi carrier formation

Nature Cell Biology volume 14, pages 343–354 (2012)Cite this article

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Abstract

Large pleiomorphic carriers leave the Golgi complex for the plasma membrane by en bloc extrusion of specialized tubular domains, which then undergo fission. Several components of the underlying molecular machinery have been identified, including those involved in the budding/initiation of tubular carrier precursors (for example, the phosphoinositide kinase PI(4)KIIIβ, the GTPase ARF, and FAPP2), and in the fission of these precursors (for example, PKD, CtBP1-S/BARS). However, how these proteins interact to bring about carrier formation is poorly understood. Here, we describe a protein complex that mediates carrier formation and contains budding and fission molecules, as well as other molecules, such as the adaptor protein 14-3-3γ. Specifically, we show that 14-3-3γ dimers bridge CtBP1-S/BARS with PI(4)KIIIβ, and that the resulting complex is stabilized by phosphorylation by PKD and PAK. Disrupting the association of these proteins inhibits the fission of elongating carrier precursors, indicating that this complex couples the carrier budding and fission processes.

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Figure 1: BARS interacts with 14-3-3γ and several proteins involved in PGC formation.
Figure 2: 14-3-3γ depletion reduces VSVG-positive PGC formation.
Figure 3: 14-3-3γ is required for BARS-dependent fission of post-Golgi carriers.
Figure 4: The 14-3-3γ dimer bridges BARS and PI(4)KIIIβ and has a role in VSVG-positive PGC formation.
Figure 5: Localization of 14-3-3γ and BARS.
Figure 6: BARS and PI(4)KIIIβ are required for Golgi localization of 14-3-3γ.
Figure 7: Molecular organization, regulation and functional role of BARS–14-3-3γ interaction.
Figure 8: 14-3-3γ is required for COPI retrograde transport and macropinocytosis, and close association of PI(4)KIIIβ and BARS at the Golgi during a traffic pulse.

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Acknowledgements

The authors would like to thank all colleagues who kindly provided them with antibodies and reagents (as listed under ‘Reagents’); M. A. De Matteis and C. Wilson for critical reading of the manuscript; J. Chernoff for the PAK inhibitor IPA-3 (Fox Chase Cancer Center); C. P. Berrie for critical reading of and editorial assistance with the manuscript; C. Cericola for preparation of the anti-BARS antibody; R. Le Donne and E. Fontana for preparation of the figures; the Integrated Microscopy Facility at the Institute of Genetics and Biophysics, National Research Council, Naples, and the Dynamic Imaging Microscopy Facility at the CEINGE Institute, Naples, for support in imaging microscopy, data processing and analysis; the Italian Association for Cancer Research (to D.C. IG4664 and IG10341, to A.L. IG4700, to A.C. IG6074 and to R.S.P. IG10233), Telethon Italia (to D.C. GGPO9274, to A.L. GGPO8231 and to R.S.P. GTF08001), the European Community Seventh Framework Programme FP7/2007-2013 HEALTH-F2-2007-201804 (Eucilia to A.L.), grant FIT DM 24/09/2009, Legge 46/82, and FaReBio, Ministry of Economy and Finance (to D.C.) for financial support. C.V., A.P. and S.S. were recipients of Italian Foundation for Cancer Research Fellowships (FIRC, Milan, Italy).

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  1. Stefania Spanò

    Present address: Present address: Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, New Haven, Connecticut 06536, USA,

Authors and Affiliations

  1. Institute of Protein Biochemistry, National Research Council, Via Pietro Castellino 111, 80131 Naples, Italy

    Carmen Valente, Gabriele Turacchio, Stefania Mariggiò, Alessandro Pagliuso, Antonino Colanzi, Alberto Luini & Daniela Corda

  2. Telethon Institute of Genetics and Medicine, Via Pietro Castellino 111, 80131 Naples, Italy

    Carmen Valente, Alessandro Pagliuso, Michele Santoro, Roman S. Polishchuk & Alberto Luini

  3. Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, Via Nazionale, 66030 Santa Maria Imbaro, Chieti, Italy

    Carmen Valente, Gabriele Turacchio, Stefania Mariggiò, Alessandro Pagliuso, Renato Gaibisso, Giuseppe Di Tullio, Michele Santoro, Stefania Spanò, Roman S. Polishchuk, Antonino Colanzi, Alberto Luini & Daniela Corda

  4. Fondazione Istituto Italiano di Tecnologia IIT@CRIB, Center for Advanced Biomaterials for Health Care, Largo Barsanti e Matteucci 53, 80125 Naples, Italy

    Fabio Formiggini

  5. CEINGE Biotecnologie Avanzate, via Gaetano Salvatore 482, 80145 Naples, Italy

    Fabio Formiggini

  6. Fondazione Istituto FIRC di Oncologia Molecolare (IFOM), IFOM-IEO, Via Adamello 16, 20139 Milan, Italy

    Daniele Piccini

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Contributions

C.V. designed, carried out and analysed all of the experiments and co-wrote the manuscript. G.T. carried out immunofluorescence and electron microscopy experiments. A.P. carried out COPI retrograde transport and macropinocytosis assays. G.D.T., M.S. and D.P. produced essential antibodies. F.F. carried out FRET and FLIM experiments. S.S. carried out initial experiments. R.G. carried out some phosphorylation experiments. R.S.P. carried out time-lapse microscopy. A.C. and S.M. contributed to relevant discussions and suggestions. D.C. and A.L. conceived and supervised the project, discussed and analysed the data and co-wrote the manuscript.

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Valente, C., Turacchio, G., Mariggiò, S. et al. A 14-3-3γ dimer-based scaffold bridges CtBP1-S/BARS to PI(4)KIIIβ to regulate post-Golgi carrier formation. Nat Cell Biol 14, 343–354 (2012). https://doi.org/10.1038/ncb2445

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