A defined tubby domain β-barrel surface region of TULP3 mediates ciliary trafficking of diverse cargoes.

ABSTRACT: The primary cilium is a paradigmatic subcellular compartment at the nexus of numerous cellular and morphogenetic pathways. The tubby family protein TULP3 acts as an adapter of the intraflagellar transport complex A in transporting integral membrane and membrane-associated lipidated proteins into cilia. However, the mechanisms by which TULP3 coordinates ciliary transport of diverse cargoes is not well understood. Here, we provide molecular insights into TULP3-mediated ciliary cargo recognition. We screened for critical TULP3 residues by proximity biotinylation-mass spectrometry, structural analysis, and testing TULP3 variants in human patients with hepatorenal fibrocystic disease and spina bifida. The TULP3 residues we identified 1) were located on one side of the β-barrel of the tub

SUBMITTER: Palicharla VR 

PROVIDER: S-EPMC11742108 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature