Abstract
SummaryCilia are small antenna-like cellular protrusions critical for many developmental signaling pathways. The ciliary protein Arl3 has been shown to act as a specific release factor for myristoylated and farnesylated ciliary cargo molecules by binding to the effectors Unc119 and PDE6δ. Here we describe a newly identified Arl3 binding partner, CCDC104/CFAP36. Biochemical and structural analyses reveal that the protein contains a BART-like domain and is called BARTL1. It recognizes an LLxILxxL motif at the N-terminal amphipathic helix of Arl3, which is crucial for the interaction with the BART-like domain but also for the ciliary localization of Arl3 itself. These results seem to suggest a ciliary role of BARTL1, and possibly link it to the Arl3 transport network. We thus speculate on a regulatory mechanism whereby BARTL1 aids the presentation of active Arl3 to its GTPase-activating protein RP2 or hinders Arl3 membrane binding in the area of the transition zone.
Highlights
Cilia are small, microtubule-based antennae-like protrusions of cells critical for the maintenance of cellular homeostasis and many developmental signaling pathways (Eggenschwiler and Anderson, 2007; Goetz and Anderson, 2010)
The ciliary protein Arl3 has been shown to act as a specific release factor for myristoylated and farnesylated ciliary cargo molecules by binding to the effectors Unc119 and PDE6d
Biochemical and structural analyses reveal that the protein contains a BART-like domain and is called BARTL1
Summary
Carolin Koerner, ..., Marius Ueffing, Karsten Boldt, Alfred Wittinghofer. Lokaj et al biochemically and structurally characterize BARTL1 as an Arl effector and speculate on its function in cilia. Highlights d Identification of a BART-like protein, CCDC104/BARTL1, as Arl binding partner d BARTL1 is a ciliary protein with transition zone localization d Complex structure shows BARTL1 binding to conserved.
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