5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n - 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n alternating site ATPase pathway, including a captive head state as an intermediate in the kinesin ATPase cycle 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n conventional kinesin is required for the microtubule plus-end accumulation of cytoplasmic dynein and dynactin but not for NUDF 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n Eh Klp5 is a divergent member of the kinesin 5 family that regulates genome content and microtubular assembly 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n in regulating plus end motility, KIF16B governs the spatial distribution of early endosomes in vivo and the balance between receptor recycling and degradation 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n Kin5 is an intraciliary transport motor 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n kinesin I and cytoplasmic dynein orchestrate glucose-stimulated insulin-containing vesicle movements in clonal MIN6 beta-cells. The majority of transport of large dense-core vesicles in beta-cells is mediated by kinesin I, whilst dynein probably contributes to the recovery of vesicles after rapid kiss-and-run exocytosis 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n kinesin MCAK/XKCM1destabilizes microtubules. Kinesin MCAK/XKCM1 is essential for controlling the distribution of microtubules by inducing their depolymerization 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n kinesin motor domain interacts with both alpha- and beta-tubulin 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n kinesin-1 supports long-range hyphal growth. Kinesin-1, kinesin-3 and myosin-V cooperate in polarized growth. Kinesin-3 participates in acid phosphatase secretion in hyphae 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n kinesin-2 is required for the normal steady-state localization of late endosomes/lysosomes but not early ensosomes or recycling endosomes. Kinesin-2 contributes significantly to the plus-end-directed movement of late endosomes and lysosomes 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n kinesin-5 Eg5 drives the sliding of microtubules depending on their relative orientation. Eg5 has the capability of simultaneously moving at about 20 nm/s towards the plus-ends of each of the two microtubules it crosslinks. For anti-parallel microtubules, this results in relative sliding at about 40 nm/s, comparable to spindle pole separation rates in vivo. Eg5 can tether microtubule plus-ends, suggesting an additional microtubule-binding mode for Eg5 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n Kip3p destabilizes microtubules by depolymerizing them. Kip3p disassembles microtubules exclusively at the plus end and depolymerizes longer microtubules faster than shorter ones 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n Kip3P is both a plus-end-specific depolymerase and a plus end-directed motor 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n monomeric kinesin Eg5 has a motor tightly bound to the microtubule during a majority of its ATPase cycle to generate and sustain force in the mitotic spindle 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n plus-end-enriched motor that targets regions of podosome turnover. Kinesin KIF1C is a central player in the microtubule-dependent regulation of podosomes. The KIF1C-myosin IIA interface may play a role in facilitating podosomes dynamics in a subcellular fine-tuned manner 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n the enzyme KIF3 promotes microtubule gliding 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n the majority of moving phagosomes are minus-end directed, the remainder moves towards microtubule plus-ends and a small subset moves bi-directionally. Minus-end movement showes pharmacological characteristics expected for dyneins, plus-end movement displayed pharmacological properties of kinesin 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n the rate of ER tubule extensions toward microtubule plus ends is lower than minus end-directed motility. Initiation of plus end-directed ER motility in somatic cytosol is likely to occur via activation of membrane-associated kinesin 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n the enzyme has a critical role during the metaphase-anaphase transition and cytokinesis. While the MKLP2 neck-linker is directed towards the microtubule plus-end in an ATP-like state, it does not fully dock along the motor domain. The footprint of the MKLP2 motor domain on the microtubule surface is altered compared to motile kinesins, and enhanced by kinesin-6-specific sequences 5.6.1.3 ATP + H2O + a kinesin associated with a microtubule at position n the Kif18A motor domain depolymerizes microtubule plus and minus ends 5.6.1.3 GTP + H2O + a kinesin associated with a microtubule at position n - 5.6.1.3 additional information animals survive lowered amounts of KIF3A and KIF3B through heterozygosity. Only in complete absence of KI3A do photoreceptor cells die, and homozygous null mutants of Kif3a are embryonic lethal in mice 5.6.1.3 additional information during morphogenesis of the Drosophila embryo mitotic spindle, KLP61F's crosslinking and sliding activities can facilitate the gradual accumulation of KLP61F within antiparallel interpolar microtubules at the equator, where the motor can generate force to drive poleward flux and pole-pole separation 5.6.1.3 additional information during the ATP-waiting state, the mobile tethered head of kinesin1 containing ADP can transiently interact with the microtubule 5.6.1.3 additional information full-length Eg5's motility comprises an unbiased, diffusive mode independent of ATP hydrolysis and a plus end-directed processive mode that requires ATP hydrolysis, Eg5 can switch from diffusive motility to directional motility upon binding to a second microtubule 5.6.1.3 additional information KIF4 regulates Gag stability and trafficking 5.6.1.3 additional information kinesin spindle protein is essential for mitotic spindle assembly in dividing human cells and is required for cell cycle progression through mitosis 5.6.1.3 additional information kinesin-2 binds the full-length variant of Hippel-Lindau tumour suppressor protein (pVHL30) in primary kidney cells, and mediate its association to microtubules 5.6.1.3 additional information kinesin-8 contributes both to chromosome congression to the metaphase plate and to the coupling of spindle microtubules to kinetochores during anaphase A 5.6.1.3 additional information KLP61F displays a 3fold higher preference for crosslinking microtubules in the antiparallel orientation, this polarity preference is observed in the presence of ADP or ATP plus AMPPNP, but not AMPPNP alone 5.6.1.3 additional information NOD binds tightly to microtubules in the nucleotide-free state, yet other nucleotide states, including adenosine-5'-(beta,gamma-imido)triphosphate, are weakened, NOD interaction with microtubules occurs slowly with weak activation of ADP product release. Upon rapid substrate binding, NOD detaches from the microtubule prior to the rate-limiting step of ATP hydrolysis. 5.6.1.3 additional information the binding of tail peptides to head dimers is fast and readily reversible, the second tail peptide in a folded kinesin-1 may be available to bind other molecules while kinesin-1 remains folded 5.6.1.3 additional information enzyme TbKIN-D associates with cytoskeletal microtubules in vivo, and TbKIN-D interacts with TbKIN-C, a kinetoplastid-specific kinesin 5.6.1.3 additional information KIF4 specifically binds to the microtubule, enzyme interaction with tubulin, the KIF4-specific Q248 and K249 form possible hydrogen bonds with Y108 of helix H3' of alpha-tubulin. Microtubule filament binding by enzyme KIF4, around the center line of the microtubule protofilament, the helix-alpha4-mediated microtubule-binding site is located and fitted into the intra-tubulin dimer groove 5.6.1.3 additional information the KVD motif of kinesin Kif2C interacts directly with tubulin. ATP hydrolysis in Kif2C is not required for tubulin release