TY - JOUR
T1 - Biased movement of monomeric kinesin-3 KLP-6 explained by a symmetric Brownian ratchet model
AU - Kita, Tomoki
AU - Sasaki, Kazuo
AU - Niwa, Shinsuke
N1 - Publisher Copyright:
© 2024 Biophysical Society
PY - 2025/1/7
Y1 - 2025/1/7
N2 - Most kinesin molecular motors dimerize to move processively and efficiently along microtubules; however, some can maintain processivity even in a monomeric state. Previous studies have suggested that asymmetric potentials between the motor domain and microtubules underlie this motility. In this study, we demonstrate that the kinesin-3 family motor protein KLP-6 can move forward along microtubules as a monomer upon release of autoinhibition. This motility can be explained by a change in length between the head and tail, rather than by asymmetric potentials. Using mass photometry and single-molecule assays, we confirmed that activated full-length KLP-6 is monomeric both in solution and on microtubules. KLP-6 possesses a microtubule-binding tail domain, and its motor domain does not exhibit biased movement, indicating that the tail domain is crucial for the processive movement of monomeric KLP-6. We developed a mathematical model to explain the biased Brownian movements of monomeric KLP-6. Our model concludes that a slight conformational change driven by neck-linker docking in the motor domain enables the monomeric kinesin to move forward if a second microtubule-binding domain exists.
AB - Most kinesin molecular motors dimerize to move processively and efficiently along microtubules; however, some can maintain processivity even in a monomeric state. Previous studies have suggested that asymmetric potentials between the motor domain and microtubules underlie this motility. In this study, we demonstrate that the kinesin-3 family motor protein KLP-6 can move forward along microtubules as a monomer upon release of autoinhibition. This motility can be explained by a change in length between the head and tail, rather than by asymmetric potentials. Using mass photometry and single-molecule assays, we confirmed that activated full-length KLP-6 is monomeric both in solution and on microtubules. KLP-6 possesses a microtubule-binding tail domain, and its motor domain does not exhibit biased movement, indicating that the tail domain is crucial for the processive movement of monomeric KLP-6. We developed a mathematical model to explain the biased Brownian movements of monomeric KLP-6. Our model concludes that a slight conformational change driven by neck-linker docking in the motor domain enables the monomeric kinesin to move forward if a second microtubule-binding domain exists.
UR - http://www.scopus.com/inward/record.url?scp=85211717238&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85211717238&partnerID=8YFLogxK
U2 - 10.1016/j.bpj.2024.11.3312
DO - 10.1016/j.bpj.2024.11.3312
M3 - Article
AN - SCOPUS:85211717238
SN - 0006-3495
VL - 124
SP - 205
EP - 214
JO - Biophysical Journal
JF - Biophysical Journal
IS - 1
ER -