Activated kinesin-1 assembles into a dimer-of-dimers
This study shows that neuronal kinesin-1 (KIF5C) forms tetramers through dimer-dimer association, with conformational activation promoting this higher-order assembly.
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Tohoku UniversityORCID 0000-0001-6919-2782Unclaimed ORCID profile · follow to get notified of new preprints
5 papers
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This study shows that neuronal kinesin-1 (KIF5C) forms tetramers through dimer-dimer association, with conformational activation promoting this higher-order assembly.
Selin Gümüşderelioğlu, Natalie Sahabandu, Daniel Elnatan…·Daniel A. Starr
The paper shows UNC-83 isoforms differentially regulate kinesin-1 and dynein to control nuclear migration directionality during development.
Rei Iguchi, Tomoki Kita, Taisei Watanabe…·Shinsuke Niwa
This study characterizes KIF1Bβ motor activity using single-molecule assays and C. elegans genetics, showing reduced activity due to a disease mutation.
Shinsuke Niwa, Taisei Watanabe, Kyoko Chiba
The paper investigates the role of the FHA domain in regulating dimerization of DmUNC-104 and links abnormal dimerization to human diseases.
Shinsuke Niwa, Natsuki Furusaki, Tomoki Kita…·Kyoko Chiba
This study shows that Kid (KIF22) forms a homodimer, moves processively along microtubules, and transports double-stranded DNA, reclassifying it as a processive and dimeric motor.