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- W2000932930 abstract "It is well known that the kinesin-1 tail domain contains a second microtubule binding-site independent of the binding-site located in the head domain (1,2), but the affinity and location of the tail-microtubule interaction on tubulin is not known. We have used fluorescence anisotropy to measure a Kd of kinesin-1 tail for microtubules in the submicromolar range, and we are currently performing experiments to determine the specific tubulin residues involved in forming this interaction. We hypothesize that the tail binding-site will include the extreme C-terminus of tubulin, which we will test by measuring the affinity of tail for tubulin with its C-terminal residues cleaved. Any effects that kinesin head domains or select microtubule-associated proteins may have on the affinity of the tail for microtubules will also be analyzed by fluorescence anisotropy, and the possibility for the tail to inhibit the ATPase activity of the head while bound to microtubules will be tested with an enzyme-coupled ATPase assay. These studies will test the hypothesis that the kinesin tail can fold over and simultaneously contact both the head domain and microtubules, producing a state in which both the ATPase activity of the head domain is inhibited and the kinesin molecule is anchored to the microtubule via its tail domain, as proposed by Dietrich et al (2).1) Navone F, Niclas J, Hom-Booher N, Sparks L, Bernstein HD, McCaffrey G, Vale RD. Cloning and expression of a human kinesin heavy chain gene: Interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells. J. Cell Bio. 117(6), 1263-1275 (1992).2) Dietrich KA, Sindelar CV, Brewer P, Downing KH, Cremo CR, Rice SE. The kineisn-1 motor protein is regulated by a direct interaction of its head and tail. Proc. Nat. Ac. Sci. 105(26), 8938-8943 (2008)." @default.
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- W2000932930 date "2009-02-01" @default.
- W2000932930 modified "2023-09-28" @default.
- W2000932930 title "Examination Of The Kinesin-1 Tail Interaction With Microtubules" @default.
- W2000932930 doi "https://doi.org/10.1016/j.bpj.2008.12.618" @default.
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