Kinesin motor mechanics: binding, stepping, tracking, gating, and limping.
By S. Block. Biophysical Journal, 2007
324 citations recorded by the source corpus.
This critical review was motivated by the 10th Biophysical Discussions meeting, “Molecular Motors: Point Counterpoint”, held in Asilomar, CA, during October 19–22, 2006. Biophysical Discussions are meetings that focus on cutting-edge or emerging topics in biophysics that can benefit from intense discussions. Streaming videos of the speaker presentations at this conference, including a synopsis of this review, are available through the Biophysical Society's web site at http://www.biophysics.org/discussions. In keeping with the spirit of a discussions meeting, I present here a personal perspective on the current state of kinesin motor mechanics. Nearly a generation has passed since the discovery of the motor named kinesin (1), and the subsequent development of the very first single-molecule gliding-filament and bead assays for motility (2,3), which helped to establish the modern field of single-molecule biophysics. Discrete steps of single molecules were first measured for kinesin (4), followed shortly thereafter by reports of similar steps for myosin (5,6). Since then, literally thousands of single-molecule experiments have been performed on a whole variety of molecular motors, all with the aim of discovering how these remarkable protein machines function. Considerable and impressive progress has been achieved, but key questions still abound, and this remains a very lively field of endeavor. I discuss below my current thinking on several questions concerned with kinesin mechanics, listed in no particular order of precedence. I wade into controversy holding no illusions that everyone will share my views on the answers to these questions, but I do hope to provoke a more thoughtful examination, and set the record straight on at least a few points. By choice, and in keeping with the topic of the meeting session where this was presented (“Motor Walking Mechanisms”), the questions that I've posed relate directly to the nanoscale mechanics of kinesin motion. However, these same questions are intimately and inevitably linked to other aspects of kinesin structure, biochemistry, and cellular function.
Subfields: Cell Biology
View Paper: https://www.semanticscholar.org/paper/af093fecf301a830d9d5abc605525f2765ca0c3d
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Citations in the corpus
- SINGLE-PARTICLE TRACKING (2009, background): “Reviews on singleparticle measurements on motor proteins include [29,81–83].”
- Stochastic mechano-chemical kinetics of molecular motors: A multidisciplinary enterprise from a physicist’s perspective (2012, background): “o the other head by a mechanism mechanism that we’ll discuss below. The mechanism of the coordination of the two heads has been at the focus of intense experimental investigation over the last decade [465, 466, 467, 468, 469, 470, 471, 472]. This coordination is now viewed as a “gating” phenomenon. ”
- Allostery and cooperativity revisited (2008, background): “It has been suggested recently, based on NMR data for dihydrofolate reductase (Boehr et al. 2006), that ligand binding does not take place in the dominant conformer but rather in a higher energy configuration that is present to a small degree in the unliganded state but has a greater affinity; a…”