Interactions between TULP3 tubby domain and ARL13B amphipathic helix promote lipidated protein transport to cilia.

ABSTRACT: The primary cilium is a nexus for cell signaling and relies on specific protein trafficking for function. The tubby family protein TULP3 transports integral membrane proteins into cilia through interactions with the intraflagellar transport complex-A (IFT-A) and phosphoinositides. It was previously shown that short motifs called ciliary localization sequences (CLSs) are necessary and sufficient for TULP3-dependent ciliary trafficking of transmembrane cargoes. However, the mechanisms by which TULP3 regulates ciliary compartmentalization of nonintegral, membrane-associated proteins and whether such trafficking requires TULP3-dependent CLSs is unknown. Here we show that TULP3 is required for ciliary transport of the Joubert syndrome-linked palmitoylated GTPase ARL13B through a CLS. An N-termi

SUBMITTER: Palicharla VR 

PROVIDER: S-EPMC10011728 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature