title: Long-range cooperative binding of kinesin to a microtubule in the presence of ATP.
abstract: Interaction of kinesin-coated latex beads with a single microtubule (MT) was directly observed by fluorescence microscopy. In the presence of ATP, binding of a kinesin bead to the MT facilitated the subsequent binding of other kinesin beads to an adjacent region on the MT that extended for micrometers in length. This cooperative binding was not observed in the presence of ADP or 5'-adenylylimidodiphosphate (AMP-PNP), where binding along the MT was random. Cooperative binding also was induced by an engineered, heterodimeric kinesin, WT/E236A, that could hydrolyze ATP, yet remained fixed on the MT in the presence of ATP. Relative to the stationary WT/E236A kinesin on a MT, wild-type kinesin bound preferentially in close proximity, but was biased to the plus-end direction. These results suggest that kinesin binding and ATP hydrolysis may cause a long-range state transition in the MT, increasing its affinity for kinesin toward its plus end. Thus, our study highlights the active involvement of MTs in kinesin motility.
authors.affiliation: Form and Function Group, PRESTO, JST, Mino, Osaka 562-0035, Japan. emuto@brain.riken.go.jp
authors.forename: Etsuko
authors.initials: E
authors.lastname: Muto
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Sakai
authors.forename: Kuniyoshi
authors.initials: K
authors.lastname: Kaseda
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000378:metabolism; D002417:Cattle; D016547:Kinesins / Q000378:metabolism*; D008863:Microspheres; D008870:Microtubules / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D000255:Adenosine Triphosphate; D016547:Kinesins
references.citation: J Mol Biol. 1997 Feb 7;265(5):553-64
references.pmid: 9048948
references.citation: Proc Natl Acad Sci U S A. 1990 Dec;87(24):10053-7
references.pmid: 2148208
references.citation: Biochemistry. 1998 Dec 22;37(51):17801-9
references.pmid: 9922146
references.citation: Science. 1999 Feb 19;283(5405):1152-7
references.pmid: 10024239
references.citation: J Biol Chem. 1951 Nov;193(1):265-75
references.pmid: 14907713
references.citation: Nature. 1999 Dec 16;402(6763):778-84
references.pmid: 10617199
references.citation: Biophys J. 2000 Feb;78(2):940-9
references.pmid: 10653806
references.citation: J Mol Biol. 2001 Oct 5;312(5):1011-26
references.pmid: 11580246
references.citation: Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):16058-63
references.pmid: 12451178
references.citation: Nat Cell Biol. 2003 Dec;5(12):1079-82
references.pmid: 14634664
references.citation: J Mol Biol. 2004 Jan 2;335(1):139-53
references.pmid: 14659746
references.citation: Nature. 1984 Jan 5-11;307(5946):58-60
references.pmid: 6537825
references.citation: J Biochem. 1986 May;99(5):1465-72
references.pmid: 2940237
references.citation: Science. 1987 Jan 9;235(4785):220-2
references.pmid: 2432661
references.citation: Nature. 1989 Nov 9;342(6246):154-8
references.pmid: 2530455
references.citation: Biophys J. 1992 Dec;63(6):1471-82
references.pmid: 1489907
references.citation: Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):6865-9
references.pmid: 8041710
references.citation: J Mol Biol. 1996 Mar 22;257(1):66-76
references.pmid: 8632460
references.citation: Annu Rev Physiol. 1996;58:703-29
references.pmid: 8815816
references.citation: Nature. 1990 Nov 22;348(6299):348-52
references.pmid: 2174512
references.citation: Biophys J. 1997 Oct;73(4):2012-22
references.pmid: 9336196