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Literature summary for 5.6.1.4 extracted from

  • Locke, J.; Joseph, A.P.; Pena, A.; Moeckel, M.M.; Mayer, T.U.; Topf, M.; Moores, C.A.
    Structural basis of human kinesin-8 function and inhibition (2017), Proc. Natl. Acad. Sci. USA, 114, E9539-E9548 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
BTB-1 BTB-1 inhibits both of the microtubule-based Kif18A activities. Allosteric BTB-1-binding site near loop5, where it blocks the ATP-dependent conformational changes Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + a kinesin associated with a microtubule at position n Homo sapiens the Kif18A motor domain depolymerizes microtubule plus and minus ends ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
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Organism

Organism UniProt Comment Textmining
Homo sapiens Q8NI77
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a kinesin associated with a microtubule at position n the Kif18A motor domain depolymerizes microtubule plus and minus ends Homo sapiens ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
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Synonyms

Synonyms Comment Organism
KIF18A
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Homo sapiens
kinesin-8
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Homo sapiens

General Information

General Information Comment Organism
physiological function Kif18A regulates spindle microtubules through its dual functionality, with microtubule-based stepping and regulation of microtubule dynamics Homo sapiens