Tubulin Acetylation Alone Does Not Affect Kinesin-1 Velocity and Run Length In Vitro

被引：77

作者：

Walter, Wilhelm J. ^{[1
]}

Beranek, Vaclav ^{[1
]}

Fischermeier, Elisabeth ^{[1
]}

Diez, Stefan ^{[1
,2
]}

机构：

[1] Tech Univ Dresden, CUBE Ctr Mol Bioengn B, D-01062 Dresden, Germany

[2] Max Planck Insitute Mol Cell Biol & Genet, Dresden, Germany

来源：

PLOS ONE | 2012年 / 7卷 / 08期

基金：

欧洲研究理事会;

关键词：

HUNTINGTONS-DISEASE; MOTOR DOMAIN; TRANSPORT; MICROTUBULES; BINDING; ACETYLTRANSFERASE; PROCESSIVITY; DEACETYLASE; MICROSCOPY; MOLECULES;

D O I：

10.1371/journal.pone.0042218

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Kinesin-1 plays a major role in anterograde transport of intracellular cargo along microtubules. Currently, there is an ongoing debate of whether alpha-tubulin K40 acetylation directly enhances the velocity of kinesin-1 and its affinity to the microtubule track. We compared motor motility on microtubules reconstituted from acetylated and deacetylated tubulin. For both, single- and multi-motor in vitro motility assays, we demonstrate that tubulin acetylation alone does not affect kinesin-1 velocity and run length.

引用

页数：5

共 30 条

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