8QAT

Cryo-EM structure of Fts-Hook3-FHIP1B at 3.2 A resolution.

8QAT の概要

• エントリーDOI: 10.2210/pdb8qat/pdb
• EMDBエントリー: 18302
• 分子名称: Protein Hook homolog 3, FHF complex subunit HOOK-interacting protein 1B, AKT-interacting protein (3 entities in total)
• 機能のキーワード: motor proteins ; molecular motors ; cargo adaptors ; bidirectional transport ; microtubules ; cytoskeleton., protein transport
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 173605.62

構造登録者

Abid Ali, F.,Carter, A.P. (登録日: 2023-08-23, 公開日: 2024-09-04, 最終更新日: 2025-04-23)

主引用文献

Abid Ali, F.,Zwetsloot, A.J.,Stone, C.E.,Morgan, T.E.,Wademan, R.F.,Carter, A.P.,Straube, A.
KIF1C activates and extends dynein movement through the FHF cargo adapter.
Nat.Struct.Mol.Biol., 32:756-766, 2025

PubMed Abstract: Cellular cargos move bidirectionally on microtubules by recruiting opposite polarity motors dynein and kinesin. These motors show codependence, where one requires the activity of the other, although the mechanism is unknown. Here we show that kinesin-3 KIF1C acts as both an activator and a processivity factor for dynein, using in vitro reconstitutions of human proteins. Activation requires only a fragment of the KIF1C nonmotor stalk binding the cargo adapter HOOK3. The interaction site is separate from the constitutive factors FTS and FHIP, which link HOOK3 to small G-proteins on cargos. We provide a structural model for the autoinhibited FTS-HOOK3-FHIP1B (an FHF complex) and explain how KIF1C relieves it. Collectively, we explain codependency by revealing how mutual activation of dynein and kinesin occurs through their shared adapter. Many adapters bind both dynein and kinesins, suggesting this mechanism could be generalized to other bidirectional complexes.

PubMed: 39747486
DOI: 10.1038/s41594-024-01418-z

実験手法

ELECTRON MICROSCOPY (3.2 Å)