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Literature summary for 5.6.1.4 extracted from

  • Hou, R.; Wang, Z.
    A coordinated molecular fishing mechanism in heterodimeric kinesin (2010), Phys. Biol., 7, 036003.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end) a molecular mechanical model for the Kar3/Vik1 heterodimer is described based on structural, kinetic and motility data revealing a long-range chemomechanical transmission mechanism that resembles a familiar fishing tactic. By this this molecular fishing, ATP-binding to Kar3 dissociates catalytically inactive Vik1 off microtubule to facilitate minus-end sliding of the dimer on the microtubule lattice. When the dimer binds the frayed ends of the microtubules, the fishing channels ATP hydrolysis energy into the microtubule depolymerization by a mechanochemical effect Saccharomyces cerevisiae

Subunits

Subunits Comment Organism
heterodimer unlike many members of the kinesin superfamily, Kar3 forms a hetereodimer with non-motor protein Vik1 or Cik1 in vivo. The heterodimers show ATP-driven minus-end directed motility along a microtubule lattice, and also serve a depolymerase at the microtubule ends Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Kar3
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Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function Kar3 is a kinesin motor that facilitates chromosome segregation during cell division Saccharomyces cerevisiae