Intramolecular Strain Coordinates Kinesin Stepping Behavior along Microtubules Export

@article{YildizA_KinesinStepBehavior_Cell_2008, abstract = {Kinesin advances 8 nm along a microtubule per ATP hydrolyzed, but the mechanism responsible for coordinating the enzymatic cycles of kinesin's two identical motor domains remains unresolved. Here, we have tested whether such coordination is mediated by intramolecular tension generated by the "neck linkers," mechanical elements that span between the motor domains. When tension is reduced by extending the neck linkers with artificial peptides, the coupling between ATP hydrolysis and forward stepping is impaired and motor's velocity decreases as a consequence. However, speed recovers to nearly normal levels when external tension is applied by an optical trap. Remarkably, external load also induces bidirectional stepping of an immotile kinesin that lacks its mechanical element (neck linker) and fuel (ATP). Our results indicate that the kinesin motor domain senses and responds to strain in a manner that facilitates its plus-end-directed stepping and communication between its two motor domains.}, address = {Department of Cellular and Molecular Pharmacology and the Howard Hughes Medical Institute, University of California, San Francisco, CA 94158, USA.}, author = {YILDIZ,, A and TOMISHIGE,, M and GENNERICH,, A and VALE,, R}, citeulike-article-id = {3326929}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.cell.2008.07.018}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0092867408009367}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/18805095}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=18805095}, day = {19}, doi = {10.1016/j.cell.2008.07.018}, issn = {00928674}, journal = {Cell}, keywords = {behavior, kinesin, stepping}, month = {September}, number = {6}, pages = {1030--1041}, posted-at = {2008-10-07 09:28:13}, priority = {0}, title = {Intramolecular Strain Coordinates Kinesin Stepping Behavior along Microtubules}, url = {http://dx.doi.org/10.1016/j.cell.2008.07.018}, volume = {134}, year = {2008} }

TY - JOUR ID - YildizA_KinesinStepBehavior_Cell_2008 L3 - citeulike-article-id:3326929 N2 - Kinesin advances 8 nm along a microtubule per ATP hydrolyzed, but the mechanism responsible for coordinating the enzymatic cycles of kinesin's two identical motor domains remains unresolved. Here, we have tested whether such coordination is mediated by intramolecular tension generated by the "neck linkers," mechanical elements that span between the motor domains. When tension is reduced by extending the neck linkers with artificial peptides, the coupling between ATP hydrolysis and forward stepping is impaired and motor's velocity decreases as a consequence. However, speed recovers to nearly normal levels when external tension is applied by an optical trap. Remarkably, external load also induces bidirectional stepping of an immotile kinesin that lacks its mechanical element (neck linker) and fuel (ATP). Our results indicate that the kinesin motor domain senses and responds to strain in a manner that facilitates its plus-end-directed stepping and communication between its two motor domains. IS - 6 JF - Cell SN - 00928674 AD - Department of Cellular and Molecular Pharmacology and the Howard Hughes Medical Institute, University of California, San Francisco, CA 94158, USA. EP - 1041 TI - Intramolecular Strain Coordinates Kinesin Stepping Behavior along Microtubules VL - 134 SP - 1030 KW - behavior KW - kinesin KW - stepping AU - YILDIZ,, A AU - TOMISHIGE,, M AU - GENNERICH,, A AU - VALE,, R PY - 2008/09/19/ UR - http://dx.doi.org/10.1016/j.cell.2008.07.018 ER -