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作 者:Guang Liu Limei Wang Junmin Pan
机构地区:[1]MOE Key Laboratory of Protein Sciences,Tsinghua-Peking Center for Life Sciences,School of Life Sciences,Tsinghua University,Beijing 100084,China [2]Laboratory for Marine Biology and Biotechnology,Qingdao National Laboratory for Marine Science and Technology,Qingdao 266200,China
出 处:《Journal of Molecular Cell Biology》2019年第9期770-780,共11页分子细胞生物学报(英文版)
基 金:the National Key R&D Program of China(2017YFA0503500);the National Natural Science Foundation of China(31330044 and 31671387)to J.P.
摘 要:The motility of cilia or eukaryotic flagella is powered by the axonemal dyneins,which are preassembled in the cytoplasm by proteins termed dynein arm assembly factors(DNAAFs)before being transported to and assembled on the ciliary axoneme.Here,we characterize the function of WDR92 in Chlamydomonas.Loss of WDR92,a cytoplasmic protein,in a mutant wdr92 generated by DNA insertional mutagenesis resulted in aflagellate cells or cells with stumpy or short flagella,disappearance of axonemal dynein arms,and diminishment of dynein arm heavy chains in the cytoplasm,suggesting that WDR92 is a DNAAF.Immunoprecipitation of WDR92 followed by mass spectrometry identified inner dynein arm heavy chains and multiple DNAAFs including RuvBLl,RPAP3,MOT48,ODA7,and DYX1C.The PIH1 domain-containing protein MOT48 formed a R2TP-like complex with RuvBLl/2 and RPAP3,while PF13,another PIH1 domain-containing protein with function in dynein preassembly,did not.Interestingly,the third PIH1 domain-containing protein TWI1 was not related to flagellar motility.WDR92 physically interacted with the R2TP-like complex and the other identified DNNAFs.Our data suggest that WDR92 functions in association with the HSP90 co-chaperone R2TP-like complex as well as linking other DNAAFs in dynein preassembly.
关 键 词:CILIA MOTILITY DYNEIN arm assembly factors R2TP COMPLEX WDR92 CHLAMYDOMONAS
分 类 号:R32[医药卫生—人体解剖和组织胚胎学]
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