The primary structure and analysis of the squid kinesin heavy chain
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Reports the cDNA sequence of squid kinesin heavy chain from D. pealeii
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Identifies head (motor), stalk (coiled-coil), and tail domains
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Motor domain is nearly neutral in charge, stalk is acidic, tail is basic
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Heptad repeat pattern in the stalk indicates coiled-coil dimerization
Quantitative measurements and modeling of cargo-motor interactions during fast transport in the living axon
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Kinesin interacts with amyloid-beta precursor-like protein (APP) in squid axon
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APP-C and negatively charged beads are transported anterogradely in the giant axon
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Quantified instantaneous/maximum velocities, run lengths, pause frequencies
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APP-C cargo achieves greater progress toward presynaptic terminal than charged beads
RNA recoding in cephalopods tailors microtubule motor protein function
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Squid kinesin-1 is extensively recoded by A-to-I RNA editing (37 sites in motor domain)
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Tissue-specific recoding generates kinesin variants with distinct motile properties
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Stellate ganglion variants display increased velocity vs optic lobe variants
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Cold-water kinesin variants show enhanced run distances and landing rates at 8C
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Cephalopod recoding sites reveal functional residues in conserved non-cephalopod motors
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Optic lobe kinesin variant has average speed ~520 nm/s vs unedited ~587 nm/s; stellate ganglion variants show increased velocities ~620-674 nm/s
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~60% of all squid mRNAs undergo A-to-I recoding, and kinesin-1 has 37 editing sites in the motor domain alone
Temperature-dependent RNA editing in octopus extensively recodes the neural proteome
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K282R editing in kinesin-1 motor domain is highly temperature-sensitive (30% shift per 10C)
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Edited kinesin-1 has lower velocity and shorter run lengths than wild-type
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Editing increases kinesin's temperature sensitivity to match cellular demand
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Temperature-dependent kinesin editing confirmed in wild-caught octopus populations
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17 recoding sites in kinesin-1 heavy chain mRNA, 8 are temperature-sensitive
Identification of molecular motors in the Woods Hole squid, Loligo pealei: an expressed sequence tag approach
Fast axonal transport in isolated axoplasm from the squid giant axon
Kinesin hydrolyses one ATP per 8-nm step.
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Each ATP hydrolyzed yields a single 8-nanometer step by kinesin along the microtubule, corresponding to the size of one tubulin dimer.
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Kinesin operates through a processive hand-over-hand mechanism where one head remains attached at all times, allowing hundreds of consecutive steps.
Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility.
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Kinesin was first discovered in squid giant axon extracts in 1985 as a soluble force-generating protein that could move organelles and beads along microtubules.
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Kinesin moves at rates of 1-2 um/second in squid axons, corresponding to fast axonal transport speeds of several hundred mm/day.
Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic assignment of GO terms using logical inference, based on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models