title: Molecular motors take tension in stride.
abstract: Mechanical tension controls the function of a wide variety of eukaryotic motor proteins. Single-molecule analyses have revealed how some of these proteins sense and respond to tension. The single motor studies on dynein by Reck-Peterson et al (2006) described in this issue pave the way to understand molecular mechanisms used by this unique machine.
authors.affiliation: Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA. jspudich@stanford.edu
authors.forename: James A
authors.initials: JA
authors.lastname: Spudich
mesh_terms: D001692:Biological Transport; D003593:Cytoplasm / Q000378:metabolism; D019281:Dimerization; D004398:Dyneins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D049452:Green Fluorescent Proteins / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism; D008956:Models, Chemical; D020409:Molecular Motor Proteins / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D045663:Quantum Dots; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism
chemical_list: D020409:Molecular Motor Proteins; D011994:Recombinant Proteins; D049452:Green Fluorescent Proteins; D004398:Dyneins