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Polyubiquitylation of alpha-tubulin at K304 is required for flagella disassembly in Chlamydomonas
Wang, Qiyu1,2; Peng, Zhao1,2; Long, Huan1; Deng, Xuan1; Huang, Kaiyao1
Corresponding AuthorHuang, Kaiyao(huangky@ihb.ac.cn)
2019-03-01
Source PublicationJOURNAL OF CELL SCIENCE
ISSN0021-9533
Volume132Issue:6Pages:12
AbstractCilia/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.
KeywordChlamydomonas Cilia Ubiquitin Cytoskeleton Organelle Intraflagellar transport
DOI10.1242/jcs.229047
Funding OrganizationNational 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
Indexed BySCI ; SCI
Language英语
Funding ProjectNational Natural Science Foundation of China[31371354] ; National Natural Science Foundation of China[31671399]
WOS Research AreaCell Biology
WOS SubjectCell Biology
WOS IDWOS:000462864300020
WOS KeywordREINHARDTII ; ELONGATION ; PROTEOMICS ; MECHANISM ; TRANSPORT ; DYNAMICS ; SYSTEM ; CILIA ; IFT
PublisherCOMPANY BIOLOGISTS LTD
Funding OrganizationNational 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
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Cited Times:4[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/342005/27873
Collection藻类生物学及应用研究中心
Corresponding AuthorHuang, Kaiyao
Affiliation1.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
Recommended Citation
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.
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