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Coupling of ATP hydrolysis to microt...

Hunter, Andrew William.

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Coupling of ATP hydrolysis to microtubule depolymerization by mitotic centromere-associated kinesin.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Coupling of ATP hydrolysis to microtubule depolymerization by mitotic centromere-associated kinesin./
Author:	Hunter, Andrew William.
Description:	109 p.
Notes:	Chair: Linda Wordeman.
Contained By:	Dissertation Abstracts International63-08B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3062952
ISBN:	0493814892

Coupling of ATP hydrolysis to microtubule depolymerization by mitotic centromere-associated kinesin.
Hunter, Andrew William.

Coupling of ATP hydrolysis to microtubule depolymerization by mitotic centromere-associated kinesin. - 109 p.

Chair: Linda Wordeman.

Thesis (Ph.D.)--University of Washington, 2002.

MCAK belongs to the Kin I subfamily of kinesin-related proteins, a unique group of motor proteins that are not motile but instead induce microtubule depolymerization. In the presence of ATP, MCAK binds to both ends of microtubules and has one high affinity site (<italic>K</italic>d = 1 nM) per protofilament end. MCAK targets microtubule ends very quickly (<italic>k</italic>on = 7.8 × 10<super>8</super> M<super> −1</super> s<super>−1</super>) by diffusion along the microtubule lattice. Once at a protofilament end MCAK acts as a processive depolymerase, removing tens of tubulin dimers, at a maximum rate of 1 s<super>−1</super> per MCAK dimer, before dissociating. MCAK has a low basal ATPase activity which is stimulated 10-fold by free tubulin and 350-fold by microtubule ends. Coupling of MCAK depolymerase activity to ATP hydrolysis revealed that five ATPs are required to remove each tubulin dimer from microtubules that resemble the GTP-cap thought to stabilize microtubules during growth. Our results show how the kinesin crossbridge cycle has been adapted to target MCAK to microtubule ends and utilize ATP hydrolysis to power microtubule depolymerization rather than directed motility.

ISBN: 0493814892Subjects--Topical Terms:

1017686
Biology, Cell.

Coupling of ATP hydrolysis to microtubule depolymerization by mitotic centromere-associated kinesin.
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020 $a 0493814892
035 $a (UnM)AAI3062952
035 $a AAI3062952
040 $a UnM $c UnM
100 1 $a Hunter, Andrew William. $3 1251300
245 1 0 $a Coupling of ATP hydrolysis to microtubule depolymerization by mitotic centromere-associated kinesin.
300 $a 109 p.
500 $a Chair: Linda Wordeman.
500 $a Source: Dissertation Abstracts International, Volume: 63-08, Section: B, page: 3547.
502 $a Thesis (Ph.D.)--University of Washington, 2002.
520 $a MCAK belongs to the Kin I subfamily of kinesin-related proteins, a unique group of motor proteins that are not motile but instead induce microtubule depolymerization. In the presence of ATP, MCAK binds to both ends of microtubules and has one high affinity site (<italic>K</italic>d = 1 nM) per protofilament end. MCAK targets microtubule ends very quickly (<italic>k</italic>on = 7.8 × 10<super>8</super> M<super> −1</super> s<super>−1</super>) by diffusion along the microtubule lattice. Once at a protofilament end MCAK acts as a processive depolymerase, removing tens of tubulin dimers, at a maximum rate of 1 s<super>−1</super> per MCAK dimer, before dissociating. MCAK has a low basal ATPase activity which is stimulated 10-fold by free tubulin and 350-fold by microtubule ends. Coupling of MCAK depolymerase activity to ATP hydrolysis revealed that five ATPs are required to remove each tubulin dimer from microtubules that resemble the GTP-cap thought to stabilize microtubules during growth. Our results show how the kinesin crossbridge cycle has been adapted to target MCAK to microtubule ends and utilize ATP hydrolysis to power microtubule depolymerization rather than directed motility.
590 $a School code: 0250.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biophysics, General. $3 1019105
690 $a 0379
690 $a 0786
710 2 0 $a University of Washington. $3 545923
773 0 $t Dissertation Abstracts International $g 63-08B.
790 $a 0250
790 1 0 $a Wordeman, Linda, $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3062952