Structural basis for Arl3-specific release of myristoylated ciliary cargo from UNC119.
作者： Shehab A Ismail , Yong-Xiang Chen , Mandy Miertzschke , Ingrid R Vetter , Carolin Koerner
关键词: Biology 、 ADP ribosylation factor 、 Cellular localization 、 Cell biology 、 Protein structure 、 Plasma protein binding 、 Small G Protein 、 Ciliary membrane 、 GTP-binding protein regulators 、 Myristoylation
摘要: Access to the ciliary membrane for trans-membrane or membrane-associated proteins is a regulated process. Previously, we have shown that closely homologous small G Arl2 and Arl3 allosterically regulate prenylated cargo release from PDEδ. UNC119/HRG4 responsible delivery of myristoylated cargo. Here, show although bind UNC119 with similar affinities, only displaces by accelerating its three orders magnitude. Crystal structures in complex UNC119a reveal molecular basis specificity. Contrary previous GTP-bound Arf subfamily proteins, N-terminal amphipathic helix Arl3·GppNHp not displaced interswitch toggle but remains bound on surface protein. Opposite mechanism PDEδ, this induces widening myristoyl binding pocket. This leads us propose targeting dependent nucleotide status also cellular localization Arl3.
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