Association of TriC/CCT with target proteins during biosynthesis / RHOBTB1 GTPase cycle / negative regulation of protein folding / RHOBTB2 GTPase cycle / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / zona pellucida receptor complex / positive regulation of establishment of protein localization to telomere / scaRNA localization to Cajal body / positive regulation of telomerase RNA localization to Cajal body / chaperonin-containing T-complex ...Association of TriC/CCT with target proteins during biosynthesis / RHOBTB1 GTPase cycle / negative regulation of protein folding / RHOBTB2 GTPase cycle / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / zona pellucida receptor complex / positive regulation of establishment of protein localization to telomere / scaRNA localization to Cajal body / positive regulation of telomerase RNA localization to Cajal body / chaperonin-containing T-complex / acetyltransferase activator activity / binding of sperm to zona pellucida / WD40-repeat domain binding / pericentriolar material / microtubule organizing center / cellular response to transforming growth factor beta stimulus / chaperone-mediated protein complex assembly / 加水分解酵素; 酸無水物に作用; リン含有酸無水物に作用 / beta-tubulin binding / heterochromatin / positive regulation of telomere maintenance via telomerase / Neutrophil degranulation / protein folding chaperone / acrosomal vesicle / mRNA 3'-UTR binding / ATP-dependent protein folding chaperone / mRNA 5'-UTR binding / response to virus / : / melanosome / myelin sheath / heparin binding / G-protein beta-subunit binding / protein folding / cell body / regulation of apoptotic process / microtubule / protein stabilization / positive regulation of apoptotic process / apoptotic process / ubiquitin protein ligase binding / positive regulation of gene expression / centrosome / Golgi apparatus / ATP hydrolysis activity / mitochondrion / DNA binding / nucleoplasm / ATP binding / metal ion binding / identical protein binding / nucleus / cytoplasm / cytosol 類似検索 - 分子機能
PDCD5-like / PDCD5-like superfamily / Double-stranded DNA-binding domain / T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit ...PDCD5-like / PDCD5-like superfamily / Double-stranded DNA-binding domain / T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit / T-complex protein 1, beta subunit / : / Chaperonins TCP-1 signature 1. / : / Chaperonins TCP-1 signature 2. / Chaperonin TCP-1, conserved site / Chaperonins TCP-1 signature 3. / Chaperone tailless complex polypeptide 1 (TCP-1) / GroEL-like equatorial domain superfamily / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / TCP-1/cpn60 chaperonin family / Chaperonin Cpn60/GroEL/TCP-1 family 類似検索 - ドメイン・相同性
T-complex protein 1 subunit alpha / T-complex protein 1 subunit theta / Programmed cell death protein 5 / T-complex protein 1 subunit eta / T-complex protein 1 subunit beta / T-complex protein 1 subunit delta / T-complex protein 1 subunit epsilon / T-complex protein 1 subunit zeta / T-complex protein 1 subunit gamma 類似検索 - 構成要素
National Natural Science Foundation of China (NSFC)
中国
引用
ジャーナル: Mol Cell / 年: 2026 タイトル: PDCD5 promotes substrate release from the TRiC complex in cilia and flagella. 著者: Huafang Wei / Qianqian Song / Liying Wang / Qiong Deng / Bingbing Wu / Yinghong Chen / Tingting Han / Yueshuai Guo / Zuyang Li / Fucheng Dong / Shuang Ma / Qiaoyu Zhao / Xiangyi Shi / Chen ...著者: Huafang Wei / Qianqian Song / Liying Wang / Qiong Deng / Bingbing Wu / Yinghong Chen / Tingting Han / Yueshuai Guo / Zuyang Li / Fucheng Dong / Shuang Ma / Qiaoyu Zhao / Xiangyi Shi / Chen Pan / Wanying Jiang / Xiaofei Liu / Yingyu Chen / Renjie Jiao / Li Yuan / Chao Liu / Xuejiang Guo / Yao Cong / Wei Li / 要旨: Approximately 10% of eukaryotic proteins are folded by the TRiC/CCT complex (TCP1-ring complex, also called CCT for cytosolic chaperonin containing TCP1), and only open-state TRiC can bind with ...Approximately 10% of eukaryotic proteins are folded by the TRiC/CCT complex (TCP1-ring complex, also called CCT for cytosolic chaperonin containing TCP1), and only open-state TRiC can bind with programmed cell death 5 (PDCD5). However, the physiological role of the PDCD5-TRiC interaction remains elusive. Here, we show that PDCD5 is required for flagellum biogenesis and ciliogenesis and present the PDCD5-TRiC structures in their open states at near-atomic resolution. Mechanically, we find that PDCD5 promotes substrates release by competing with PhLP2A to interact with TRiC, and the depletion of PDCD5 traps flagellum- and cilium-associated proteins within TRiC, finally leading to malformed flagella of spermatids and cilia in mouse ciliated cells. Moreover, we demonstrate that the function of PDCD5 in flagellum biogenesis and ciliogenesis depends on the interaction with TRiC by its C terminus. These findings identify PDCD5 as a TRiC regulator to promote a subset of proteins release.