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Literature summary for 5.6.1.4 extracted from

  • Chu, H.M.; Yun, M.; Anderson, D.E.; Sage, H.; Park, H.W.; Endow, S.A.
    Kar3 interaction with Cik1 alters motor structure and function (2005), EMBO J., 24, 3214-3223.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.4

Activating Compound

Activating Compound Comment Organism Structure
Cik1 Cik1 and Kar3 stalk regions preferentially associate with one another rather than forming homodimers. Kar3/Cik1 moves on microtubules at 0.002-0.0024 mm/min, 2-5fold faster than Kar3, and destabilizes microtubules at the lagging ends. Structural changes in Kar3 upon dimerization with Cik1 alter the motor velocity and likely regulate Kar3 activity in vivo Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
His6Kar3/Cik1-S tag protein Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
15000
-
 His6Kar3/Cik1-S tag protein, gel filtration Saccharomyces cerevisiae

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 Saccharomyces cerevisiae
-
 ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
His6Kar3/Cik1-S tag protein Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a kinesin associated with a microtubule at position n
-
 Saccharomyces cerevisiae ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
 ?

Subunits

Subunits Comment Organism
More Cik1 and Kar3 stalk regions preferentially associate with one another rather than forming homodimers. Kar3/Cik1 moves on microtubules at 0.002-0.0024 mm/min, 2-5fold faster than Kar3, and destabilizes microtubules at the lagging ends. Structural changes in Kar3 upon dimerization with Cik1 alter the motor velocity and likely regulate Kar3 activity in vivo Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Kar3
-
 Saccharomyces cerevisiae