9IKB

Crystal structure of heterotrimeric Kinesin-2

Summary for 9IKB

• Entry DOI: 10.2210/pdb9ikb/pdb
• Descriptor: Kinesin-like protein, Kinesin-like protein klp-20, Kinesin-associated protein (3 entities in total)
• Functional Keywords: kineisin, transport protein
• Biological source: Caenorhabditis elegans; More
• Total number of polymer chains: 3
• Total formula weight: 108933.51

Authors

Ren, J.,Zhao, L.,Feng, W. (deposition date: 2024-06-27, release date: 2025-07-02, Last modification date: 2026-01-14)

Primary citation

Ren, J.,Zhao, L.,Chen, G.,Ou, G.,Feng, W.
A mutual co-recognition mechanism ensures the proper assembly of heterotrimeric kinesin-2 for intraflagellar transport.
Nat Commun, 16:6816-6816, 2025

PubMed Abstract: Heterotrimeric kinesin-2, composed of two distinct kinesin motors and a kinesin-associated protein (KAP), is essential for intraflagellar transport and ciliogenesis. KAP specifically recognizes the hetero-paired motor tails for the holoenzyme assembly, but the underlying mechanism remains unclear. Here, we determine the structure of KAP-1 in complex with the hetero-paired tails from kinesin-2 motors KLP-20 and KLP-11. KAP-1 forms an elongated superhelical structure characterized by a central groove and a C-terminal helical (CTH)-hook. The two motor tails fold together and are co-recognized by the central groove of KAP-1. The adjacent hetero-pairing trigger sequences preceding the two tails form an intertwined heterodimer, which co-captures the CTH-hook of KAP-1 to complete the holoenzyme assembly. Mutations in the interfaces between KAP-1 and the two tails disrupt the heterotrimeric kinesin-2 complex and impair kinesin-2-mediated intraflagellar transport. Thus, KAP-1 and the hetero-paired motors are mutually co-recognized, ensuring the proper assembly of heterotrimeric kinesin-2 for cargo transport.

PubMed: 40707480
DOI: 10.1038/s41467-025-62152-8

Experimental method

X-RAY DIFFRACTION (3.54 Å)