ArticleProtein science : a publication of the Protein Society2021
Modeling processive motion of kinesin-13 MCAK and kinesin-14 Cik1-Kar3 molecular motors.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 10 citations in OpenAlex.
- Biased movement of monomeric kinesin-3 KLP-6 explained by a symmetric Brownian ratchet model.Biophysical journal · 2025Article
- Modeling study of kinesin-13 MCAK microtubule depolymerase.European biophysics journal : EBJ · 2024Article
- Modeling Studies of the Mechanism of Context-Dependent Bidirectional Movements of Kinesin-14 Motors.Molecules (Basel, Switzerland) · 2024Article
- Modeling processive motion of kinesin-13 MCAK and kinesin-14 Cik1-Kar3 molecular motors.Protein science : a publication of the Protein Society · 2021Article
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1 author at 1 institution in 2 countries.
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Abstract
Kinesin-13 MCAK, which is composed of two identical motor domains, can undergo unbiased one-dimensional diffusion on microtubules. Kinesin-14 Cik1-Kar3, which is composed of a Kar3 motor domain and a Cik1 motor homology domain with no ATPase activity, can move processively toward the minus end of microtubules. Here, we present a model for the diffusion of MCAK homodimer and a model for the processive motion of Cik1-Kar3 heterodimer. Although the two dimeric motors show different domain composition, in the models it is proposed that the two motors use the similar physical mechanism to move processively. With the models, the dynamics of the two dimers is studied analytically. The theoretical results for MCAK reproduce quantitatively the available experimental data about diffusion constant and lifetime of the motor bound to microtubule in different nucleotide states. The theoretical results for Cik1-Kar3 reproduce quantitatively the available experimental data about load dependence of velocity and explain consistently the available experimental data about effects of the exchange and mutation of the motor homology domain on the velocity of the heterodimer. Moreover, predicted results for other aspects of the dynamics of the two dimers are provided.
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