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| Title | A mutual co-recognition mechanism ensures the proper assembly of heterotrimeric kinesin-2 for intraflagellar transport. |
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| Journal, issue, pages | Nat Commun, Vol. 16, Issue 1, Page 6816, Year 2025 |
| Publish date | Jul 24, 2025 |
Authors | Jinqi Ren / Lingyan Zhao / Guanghan Chen / Guangshuo Ou / Wei Feng / ![]() |
| 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 ...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. |
External links | Nat Commun / PubMed:40707480 / PubMed Central |
| Methods | EM (single particle) / X-ray diffraction |
| Resolution | 3.54 - 4.39 Å |
| Structure data | ![]() EMDB-64192: Cryo-EM structure of the heterotrimeric kinesin-2 from Caenorhabditis elegans ![]() PDB-9ikb: |
| Source |
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Keywords | TRANSPORT PROTEIN / Kineisin |
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