2026-10-11T01:01:55Z https://api.figshare.com/v2/oai

oai:figshare.com:article/34047156 2026-10-01T16:36:29Z portal_1197 item_type_6 month_year_10_2026

KIF1C activates and extends dynein movement through the FHF cargo adaptor Ferdos Abid Ali (25017073) Alexander J. Zwetsloot (9409195) Caroline E. Stone (23775950) Tomos E. Morgan (4875328) Richard F. Wademan (14249975) Andrew P. Carter (8880857) Anne Straube (9409198) Microtubules Dynein -- Movements Kinesin Membrane proteins Cell organelles Migrated from ePrints Cellular cargos move bidirectionally on microtubules by recruiting opposite polarity motors dynein and kinesin. These motors show co-dependence, where one requires the activity of the other, although the mechanism is unknown. Here, using in vitro reconstitutions, we show the kinesin-3 KIF1C acts both as an activator and processivity factor for dynein. Activation requires only a fragment of the non-motor tail of KIF1C (KIF1C-stalk) binding the cargo adaptor 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 auto-inhibited FTS- HOOK3-FHIP1B (FHF) and explain how KIF1C relieves it. Collectively, we explain co-dependency by revealing how mutual activation of dynein and kinesin occurs through their shared adaptor. Many adaptors bind both dynein and kinesins, suggesting this mechanism could be generalised to other bidirectional complexes. 2025-04-01T00:00:00Z Text Journal contribution 10.1038/s41594-024-01418-z https://figshare.com/articles/journal_contribution/KIF1C_activates_and_extends_dynein_movement_through_the_FHF_cargo_adaptor/34047156 CC BY 4.0