| First Author | Lokaj M | Year | 2015 |
| Journal | Structure | Volume | 23 |
| Issue | 11 | Pages | 2122-32 |
| PubMed ID | 26455799 | Mgi Jnum | J:247391 |
| Mgi Id | MGI:5925653 | Doi | 10.1016/j.str.2015.08.016 |
| Citation | Lokaj M, et al. (2015) The Interaction of CCDC104/BARTL1 with Arl3 and Implications for Ciliary Function. Structure 23(11):2122-32 |
| abstractText | Cilia 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 PDE6delta. 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. |
