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

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

Research output: Contribution to journalArticlepeer-review

69 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)343-354
Number of pages12
JournalNature Cell Biology
Issue number4
Early online date26 Feb 2012
Publication statusPublished - Apr 2012


  • 14-3-3 proteins
  • alcohol oxidoreductases
  • animals
  • COS cells
  • carrier proteins
  • cercopithecus aethiops
  • DNA-binding proteins
  • dimerization
  • golgi apparatus
  • humans
  • phosphorylation
  • phosphotransferases (alcohol group acceptor)
  • protein kinase C
  • rats
  • p21-activated kinases


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