Polyubiquitylation of alpha-tubulin at K304 is required for flagella disassembly in Chlamydomonas
文献类型：期刊论文
| 作者 | Wang, Qiyu1,2; Peng, Zhao1,2; Long, Huan1; Deng, Xuan1; Huang, Kaiyao1 |
| 刊名 | JOURNAL OF CELL SCIENCE
 |
| 出版日期 | 2019-03-01 |
| 卷号 | 132期号:6页码:12 |
| 关键词 | Chlamydomonas Cilia Ubiquitin Cytoskeleton Organelle Intraflagellar transport |
| ISSN号 | 0021-9533 |
| DOI | 10.1242/jcs.229047 |
| 通讯作者 | Huang, Kaiyao(huangky@ihb.ac.cn) |
| 英文摘要 | Cilia/flagella are structurally conserved and dynamic organelles; their assembly and disassembly are coordinated with the cell cycle and cell differentiation. Several post-translational modifications, including acetylation, methylation, phosphorylation and ubiquitylation, participate in ciliary disassembly. However, the detailed mechanism and the role of ubiquitylation in ciliary disassembly are unclear. This study identified 20 proteins that were ubiquitylated in shortening flagella of Chlamydomonas. alpha-Tubulin was the most abundant ubiquitylated protein and it was labeled with K63 polyubiquitin chains primarily at K304. Expression of an a-tubulin mutant (K304R), which could not be ubiquitylated, decreased the rate of flagellar disassembly and resulted in an enrichment of the mutant form in the axoneme, suggesting that ubiquitylation of alpha-tubulin is required for the normal kinetics of axonemal disassembly. Immunoprecipitation and glutathione-S-transferase pulldown assays demonstrated that the retrograde intraflagellar transport (IFT) protein, IFT139, interacted with a variety of ubiquitylated proteins, including alpha-tubulin, suggesting that IFT-A was responsible for transporting ubiquitylated proteins out of the flagella. Our data suggest an important role for ubiquitylation and retrograde IFT in ciliary disassembly. This article has an associated First Person interview with the first author of the paper. |
| WOS关键词 | REINHARDTII ; ELONGATION ; PROTEOMICS ; MECHANISM ; TRANSPORT ; DYNAMICS ; SYSTEM ; CILIA ; IFT |
| 资助项目 | National Natural Science Foundation of China[31371354] ; National Natural Science Foundation of China[31671399] |
| WOS研究方向 | Cell Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000462864300020 |
| 出版者 | COMPANY BIOLOGISTS LTD |
| 资助机构 | National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China |
| 源URL | [http://ir.ihb.ac.cn/handle/342005/27872]  |
| 专题 | 水生生物研究所_藻类生物学及应用研究中心 |
| 通讯作者 | Huang, Kaiyao |
| 作者单位 | 1.Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Hubei, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100039, Peoples R China |
| 推荐引用方式 GB/T 7714 | Wang, Qiyu,Peng, Zhao,Long, Huan,et al. Polyubiquitylation of alpha-tubulin at K304 is required for flagella disassembly in Chlamydomonas[J]. JOURNAL OF CELL SCIENCE,2019,132(6):12. |
| APA | Wang, Qiyu,Peng, Zhao,Long, Huan,Deng, Xuan,&Huang, Kaiyao.(2019).Polyubiquitylation of alpha-tubulin at K304 is required for flagella disassembly in Chlamydomonas.JOURNAL OF CELL SCIENCE,132(6),12. |
| MLA | Wang, Qiyu,et al."Polyubiquitylation of alpha-tubulin at K304 is required for flagella disassembly in Chlamydomonas".JOURNAL OF CELL SCIENCE 132.6(2019):12. |
入库方式： OAI收割
来源：水生生物研究所
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