東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back to Search results for [ null ]

Switch To: Labeled | MARC Mode | ISBD

Tail- and light chain-mediated regul...

Wong, Yao Liang.

Linked to FindBook

Google Book

Amazon

博客來

Tail- and light chain-mediated regulation of the kinesin-1 motor.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Tail- and light chain-mediated regulation of the kinesin-1 motor./
Author:	Wong, Yao Liang.
Description:	235 p.
Notes:	Source: Dissertation Abstracts International, Volume: 71-05, Section: B, page: 2781.
Contained By:	Dissertation Abstracts International71-05B.
Subject:	Biology, Molecular. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3402502
ISBN:	9781109746280

Tail- and light chain-mediated regulation of the kinesin-1 motor.
Wong, Yao Liang.

Tail- and light chain-mediated regulation of the kinesin-1 motor. - 235 p.

Source: Dissertation Abstracts International, Volume: 71-05, Section: B, page: 2781.

Thesis (Ph.D.)--Northwestern University, 2010.

The kinesin-1 motor hydrolyzes ATP and transports cargo along microtubules (MTs). Kinesin-1's remarkable ability to regulate itself ensures proper localization of the motor and associated cargoes. To determine the mechanism of kinesin-1 auto-inhibition, we studied its regulatory elements -- the kinesin heavy chain (KHC) tail and the kinesin light chains (KLCs).

ISBN: 9781109746280Subjects--Topical Terms:

1017719
Biology, Molecular.

Tail- and light chain-mediated regulation of the kinesin-1 motor.
LDR:03596nam 2200373 4500 001 1404539
005 20111130124030.5
008 130515s2010 ||||||||||||||||| ||eng d
020 $a 9781109746280
035 $a (UMI)AAI3402502
035 $a AAI3402502
040 $a UMI $c UMI
100 1 $a Wong, Yao Liang. $3 1683867
245 1 0 $a Tail- and light chain-mediated regulation of the kinesin-1 motor.
300 $a 235 p.
500 $a Source: Dissertation Abstracts International, Volume: 71-05, Section: B, page: 2781.
500 $a Adviser: Sarah E. Rice.
502 $a Thesis (Ph.D.)--Northwestern University, 2010.
520 $a The kinesin-1 motor hydrolyzes ATP and transports cargo along microtubules (MTs). Kinesin-1's remarkable ability to regulate itself ensures proper localization of the motor and associated cargoes. To determine the mechanism of kinesin-1 auto-inhibition, we studied its regulatory elements -- the kinesin heavy chain (KHC) tail and the kinesin light chains (KLCs).
520 $a The kinesin-1 tail inhibits ATPase activity by binding to the enzymatic KHC heads. We used electron paramagnetic resonance and fluorescence spectroscopy to examine this interaction. We discovered that the mobility of spin-labeled probes in the kinesin-1 nucleotide pocket is restricted upon head-tail binding. This restriction is distinct from MT-induced changes, occurs independent of nucleotide state, and does not stabilize Mg2+ in the pocket. A K922A mutation in the tail's conserved IAK motif does not compromise head-tail binding, but completely abolishes its regulatory activity. Our results suggest that the tail scaffolds around the head to position K922 for inhibition, possibly by interacting with the nucleotide alpha/beta-phosphates in a manner analogous to the arginine finger regulators of some G-proteins.
520 $a The head-binding site in the KHC tail also mediates tail-MT interactions, possibly allowing kinesin-1 to slide/transport MTs. Surprisingly, we found that KLCs inhibit both tail-head and tail-MT binding. Fluorescence anisotropy and coupled-enzyme assays showed that KLCs reduce the affinity of the head-tail interaction 11-fold and concomitantly repress the tail's regulatory activity. We also showed that KLCs block tail-MT binding by a separate mechanism. Inhibition of head-tail binding requires steric and electrostatic factors. Inhibition of tail-MT binding is largely electrostatic, pH-dependent and mediated partly by a negatively-charged linker region of the KLCs. The data suggest that KLCs promote activation of kinesin-1 for cargo transport by suppressing tail-head and tail-MT interactions.
520 $a In conclusion, we have shown that KHC tails regulate kinesin-1 activity in a specific manner, and the tails are regulated in turn by the KLCs. Our results also demonstrate that tail's head/MT-binding site is an important regulatory focal point that may be modulated by intrinsic as well as extrinsic factors. Our work on the interplay between tails and KLCs establishes a system that may be used to assay the contributions of other kinesin-1 regulators.
590 $a School code: 0163.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biophysics, General. $3 1019105
690 $a 0307
690 $a 0379
690 $a 0786
710 2 $a Northwestern University. $b Integrated Graduate Program in the Life Sciences. $3 1682749
773 0 $t Dissertation Abstracts International $g 71-05B.
790 1 0 $a Rice, Sarah E., $e advisor
790 1 0 $a Gelfand, Vladimir I. $e committee member
790 1 0 $a Bartles, James R. $e committee member
790 1 0 $a Green, Kathleen J. $e committee member
790 1 0 $a Binder, Lester I. $e committee member
790 $a 0163
791 $a Ph.D.
792 $a 2010
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3402502