alpha 1A and alpha 1C form microtubules to display distinct properties mainly mediated by their C-terminal tails

doi:10.1093/jmcb/mjab062

	alpha 1A and alpha 1C form microtubules to display distinct properties mainly mediated by their C-terminal tails
	Diao, Lei 1; Liu, Ming-Yi1,2 ; Song, Yin-Long 3; Zhang, Xu2,4 ; Liang, Xin 3; Bao, Lan1,2
	2021-12
发表期刊	JOURNAL OF MOLECULAR CELL BIOLOGY (IF:5.3[JCR-2023],6.1[5-Year])
ISSN	1674-2788
EISSN	1759-4685
卷号	13 期号:12
发表状态	已发表
DOI	10.1093/jmcb/mjab062
摘要	Microtubules consisting of alpha/beta-tubulin dimers play critical roles in cells. More than seven genes encode alpha-tubulin in vertebrates. However, the property of microtubules composed of different alpha-tubulin isotypes is largely unknown. Here, we purified recombinant tubulin heterodimers of mouse alpha-tubulin isotypes including alpha 1A and alpha 1C with beta-tubulin isotype beta 2A. In vitro microtubule reconstitution assay detected that alpha 1C/beta 2A microtubules grew faster and underwent catastrophe less frequently than alpha 1A/beta 2A microtubules. Generation of chimeric tail-swapped and point-mutation tubulins revealed that the carboxyl-terminal (C-terminal) tails of alpha-tubulin isotypes largely accounted for the differences in polymerization dynamics of alpha 1A/beta 2A and alpha 1C/beta 2A microtubules. Kinetics analysis showed that in comparison to alpha 1A/beta 2A microtubules, alpha 1C/beta 2A microtubules displayed higher on-rate, lower off-rate, and similar GTP hydrolysis rate at the plus-end, suggesting a contribution of higher plus-end affinity to faster growth and less frequent catastrophe of alpha 1C/beta 2A microtubules. Furthermore, EB1 had a higher binding ability to alpha 1C/beta 2A microtubules than to alpha 1A/beta 2A ones, which could also be attributed to the difference in the C-terminal tails of these two alpha-tubulin isotypes. Thus, alpha-tubulin isotypes diversify microtubule properties, which, to a great extent, could be accounted by their C-terminal tails.
关键词	alpha-tubulin isotype microtubule dynamics TIRF
URL	查看原文
收录类别	SCI ; SCIE
语种	英语
资助项目	National Natural Science Foundation of China[31991194,31330046,31922018] ; Strategic Priority Research Program of Chinese Academy of Sciences[XDB19000000]
WOS研究方向	Cell Biology
WOS类目	Cell Biology
WOS记录号	WOS:000761453100003
出版者	OXFORD UNIV PRESS
引用统计	正在获取...
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/165004
专题	生命科学与技术学院_博士生生命科学与技术学院_特聘教授组_鲍岚组生命科学与技术学院_特聘教授组_张旭组
通讯作者	Liang, Xin; Bao, Lan
作者单位	1.Chinese Acad Sci, Univ Chinese Acad Sci, Ctr Excellence Mol Cell Sci, State Key Lab Cell Biol,Shanghai Inst Biochem & C, Shanghai 200031, Peoples R China 2.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 201210, Peoples R China 3.Tsinghua Univ, Tsinghua Peking Joint Ctr Life Sci, Sch Life Sci, Beijing 100084, Peoples R China 4.Chinese Acad Sci, Shanghai Adv Res Inst, Shanghai 201210, Peoples R China
通讯作者单位	生命科学与技术学院
推荐引用方式 GB/T 7714	Diao, Lei,Liu, Ming-Yi,Song, Yin-Long,et al. alpha 1A and alpha 1C form microtubules to display distinct properties mainly mediated by their C-terminal tails[J]. JOURNAL OF MOLECULAR CELL BIOLOGY,2021,13(12).
APA	Diao, Lei,Liu, Ming-Yi,Song, Yin-Long,Zhang, Xu,Liang, Xin,&Bao, Lan.(2021).alpha 1A and alpha 1C form microtubules to display distinct properties mainly mediated by their C-terminal tails.JOURNAL OF MOLECULAR CELL BIOLOGY,13(12).
MLA	Diao, Lei,et al."alpha 1A and alpha 1C form microtubules to display distinct properties mainly mediated by their C-terminal tails".JOURNAL OF MOLECULAR CELL BIOLOGY 13.12(2021).