Control of motor landing and processivity by the CAP-Gly domain in the KIF13B tail

• Published in: Nature communications 2023-08, Vol.14 (1), p.4715-4715, Article 4715
• Main Authors: Fan, Xiangyu, McKenney, Richard J.
• Format: Article
• Language: English
• Subjects: 14/35; 631/45/56; 631/45/612/1228; 631/57/2265; 631/80/128/1653; 82/83; Adenosine diphosphate; Cytoskeleton; Homeostasis; Humanities and Social Sciences; Kinesin; Kinesins - genetics; Kinesins - metabolism; Microtubule-associated proteins; Microtubule-Associated Proteins - metabolism; Microtubules - metabolism; Motility; Motor task performance; multidisciplinary; Protein Processing, Post-Translational; Science; Science (multidisciplinary); Tubulin; Tubulin - metabolism; Tyrosine
• ISSN: 2041-1723; 2041-1723
• DOI: 10.1038/s41467-023-40425-4

Microtubules are major components of the eukaryotic cytoskeleton. Posttranslational modifications (PTMs) of tubulin regulates interactions with microtubule-associated proteins (MAPs). One unique PTM is the cyclical removal and re-addition of the C-terminal tyrosine of α-tubulin and MAPs containing CAP-Gly domains specifically recognize tyrosinated microtubules. KIF13B, a long-distance transport kinesin, contains a conserved CAP-Gly domain, but the role of the CAP-Gly domain in KIF13B’s motility along microtubules remains unknown. To address this, we investigate the interaction between KIF13B’s CAP-Gly domain, and tyrosinated microtubules. We find that KIF13B’s CAP-Gly domain influences the initial motor-microtubule interaction, as well as processive motility along microtubules. The effect of the CAP-Gly domain is enhanced when the motor domain is in the ADP state, suggesting an interplay between the N-terminal motor domain and C-terminal CAP-Gly domain. These results reveal that specialized kinesin tail domains play active roles in the initiation and continuation of motor movement. Intracellular transport of material along microtubules by kinesin motors is critical for cellular homeostasis. Here the authors uncover a unique role for a specialized kinesin tail domain in directing motor transport along specific microtubule tracks.