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| 1 | Mitosis-specific acetylation tunes Ran effector binding for chromosome segregation显示文摘在房间期间,分割要求忠诚有丝分裂的锭子汇编和染色体分离的基因信息的稳定的传播。运用了 GTPase 戏在有丝分裂的锭子汇编的一个关键角色。然而,在锭子的 Ran-GTP 的一个化学坡度的产生怎么被联合到有丝分裂的 translational 以后修正,从来没被描绘过。这里,我们解决了复杂结构与核苷酸版本因素 Mog1 跑了并且描出一个新奇有丝分裂特定的调整 acetylation 的 Ran-Mog1 相互作用在染色体分离期间。我们的指导结构的功能的分析表明那 Mog1 与 RCC1 竞争为以一种 GTP/GDP-dependent 方式变有约束力。生物化学的描述表明了那 Mog1 固定跑阻止 RCC1 有约束力、随后的 GTP 装载。令人惊讶地,跑了是 TIP60 的真正的底层,并且由 TIP60 的 Lys134 的 acetylation 解放 Mog1 从在有丝分裂期间变有约束力。重要地,这个得到 acetylation 的开关对 RCC1 变有约束力支持 Ran-GTP 的高水平,它为染色体排列是必要的。这些结果建立一以前 TIP60 由调节在提供 Ran-GTP 水平的 homeostatic 控制的规章的机制运用了的 uncharacterized 为在有丝分裂的染色体分离的受动器绑定。 | Xiaoling Bao Heng Liu Xing Liu Ke Ruan Yonshui Zhang Zhiyong Zhang Qi Hu Ying Liu Saima Akram Jiahai Zhang Qingguo Gong Wenwen wang Xiao Yuan Jian-Li Lingli Zhao Zhen Dou Ruijun Tian Xuebiao Yao Jihui Wu Yunyu Shi | 2018 | Journal of Molecular Cell Biology2018，10，1： | 8 |
| 2 | Efficacy and safety of low-dose interleukin-2 in combination with methotrexate in patients with active rheumatoid arthritis:a randomized,double-blind,placebo-controlled phase 2 trial显示文摘Rheumatoid arthritis(RA)is an aggressive autoimmune arthritis,and current therapies remain unsatisfactory due to low remission rate and substantially adverse effects.Low-dose interleukin-2(Ld-IL2)is potentially a therapeutic approach to further improve the disease.This randomized,double-blind,placebo-controlled trial was undertaken to evaluate the efficacy and safety of Ld-IL2 in patients with active RA.Patients were randomly assigned(1:1)to receive Ld-IL2,defined as a dose of 1 million IU,or placebo in a 12-week trial with a 12-week follow-up.Three cycles of Ld-IL2 or placebo were administered subcutaneously every other day for 2 weeks(a total of 7 doses),followed by a 2-week break.All patients received a stable dose of methotrexate(MTX).The primary outcomes were the proportion of patients achieving the ACR20,DAS28-ESR<2.6,and the change from baseline in CDAI or SDAI at week 24.Secondary endpoints included other clinical responses and safety.The primary outcomes were achieved in the perprotocol population.The improvements from baseline in CDAI and SDAI were significantly greater across time points for the LdIL2+MTX group(n=17)than for the placebo+MTX group(n=23)(P=0.018 and P=0.015,respectively).More patients achieved ACR20 response in the Ld-IL2+MTX group than those in the placebo+MTX group at week 12(70.6%vs 43.5%)and at week 24(76.5%vs 56.5%)(P=0.014).In addition,low Treg and high IL-21 were associated with good responses to Ld-IL2.Ld-IL-2 treatment was well-tolerated in this study.These results suggested that Ld-IL2 was effective and safe in RA.ClinicalTrials.gov number:NCT 02467504. | Xiaoying Zhang Miao Miao Ruijun Zhang Xu Liu Xiaozhen Zhao Miao Shao Tian Liu Yuebo Jin Jiali Chen Huixin Liu Xia Zhang Yun Li Yunshan Zhou Yue Yang Ru Li Haihong Yao Yanying Liu Chun Li Yuhui Li Limin Ren Yin Su Xiaolin Sun Jing He Zhanguo Li | 2022 | Signal Transduction and Targeted Therapy2022，7，4： | 7 |
| 3 | CaMKIIα-driven,phosphatase-checked postsynaptic plasticity via phase separation显示文摘Ca^(2+)/calmodulin-dependent kinase Ila(CaMKIla)is essential for synaptic plasticity and learning by decoding synaptic Ca^(2+)oscillations.Despite decades of extensive research,new mechanisms underlying CaMKIIa's function in synapses are still being discovered.Here,we discover that Shank3 is a specific binding partner for autoinhibited CaMKIla.We demonstrate that Shank3 and GluN2B,via combined actions of Ca^(2+)and phosphatases,reciprocally bind to CaMKIla.Under basal condition,CaMKIla is recruited to the Shank3 subcompartment of postsynaptic density(PSD)via phase separation.Rise of Ca^(2+)concentration induces GluN2Bmediated recruitment of active CaMKIla and formation of the CaMKIIa/GluN2B/PSD-95 condensates,which are autonomously dispersed upon Ca^(2+)removal.Protein phosphatases control the Ca^(2+)-dependent shuttling of CaMKIla between the two PSD subcompartme nts and PSD condensate formation.Activation of CaMKIla further enlarges the PSD assembly and in duces structural LTP.Thus,Ca^(2+)-induced and phosphatase-checked shuttling of CaMKIla between distinct PSD nano-domains can regulate phase separation-mediated PSD assembly and synaptic plasticity. | Qixu Caic Menglong Zeng Xiandeng Wu Haowei Wu Yumeng Zhan Ruijun Tian Mingjie Zhang | 2021 | Cell Research2021，31，1： | 3 |
| 4 | Acetytation of ACAP4 regutates CCL18-elicited breast cancer cell migration and invasion显示文摘Tumor metastasis represents the main causes of cancer-related death.Our recent study showed that chemokine CCL18 secreted from tumor-associated macrophages regulates breast tumor metastasis,but the underlying mechanisms remain less clear.Here, we show that ARF6 GTPase-activating protein ACAP4 regulates CCL18-elicited breast cancer cell migration via the acetyltransferase PCAF-mediated acetylation.CCL18 stimulation elicited breast cancer cell migration and invasion via PCAF-dependent acetylation.ACAP4 physically interacts with PCAF and is a cognate substrate of PCAF during CCL18 stimulation.The acetylation site of ACAP4 by PCAF was mapped to Lys311 by mass spectrometric analyses.Importantly,dynamic acetylation of ACAP4 is essential for CCL18-induced breast cancer cell migration and invasion,as overexpression of the persistent acetylation-mimicking or nonacetylatable ACAP4 mutant blocked CCL18-elicited cell migration and invasion.Mechanistically,the acetylation of ACAP4 at Lys311 reduced the lipid-binding activity of ACAP4 to ensure a robust and dynamic cycling of ARF6-ACAP4 complex with plasma membrane in response to CCL18 stimulation.Thus,these results present a previously undefined mechanism by which CCL18-elicited acetylation of the PH domain controls dynamic interaction between ACAP4 and plasma membrane during breast cancer cell migration and invasion. | Xiaoyu Song Wei Liu Xiao Yuan Jiying Jiang Wanjuan Wang McKay Mullen Xuannv Zhao Yin Zhang Fusheng Liu Shihao Du Adeel Rehman Ruijun Tian Jian Li Andra Frost Zhenwei Song Hadiyah-Nicole Green Calmour Henry Xing Liu Xia Ding Dongmei Wang Xuebiao Yao | 2018 | Journal of Molecular Cell Biology2018，10，6： | 3 |
| 5 | 显示文摘 | TIAN Ruijun SUN Junming ZHANG He YE Mingliang XIE Chuanhui DONG Jin HU Jiwei MA Ding BAO Xinhe ZOU Hanfa | 2006 | Electrophoresis2006，27，4： | 1 |
| 6 | 显示文摘 | HU Jiwei XIE Chuanhui TIAN Ruijun | 2007 | J Sep Sci2007，30，6： | 1 |
| 7 | Combining Metabolic Alkyne Labeling and Click Chemistry for Secretome Analysis of Serum-Containing Conditioned Medium显示文摘Main observation and conclusion Bioorthogonal click chemistry has emerged as a powerful tool for the specific modification of proteins in complex mixtures.Metabolic labeling of proteins with azide followed by the copper-catalyzed azide−alkyne cycloaddition(CuAAC)with alkyne-based affinity probes/beads is widely applied to study protein turnover and post-translational modifications(PTMs). | Jiangnan Zheng Yuan Mao Shun Feng Ruijun Tian | 2021 | Chinese Journal of Chemistry2021，39，7： | 0 |
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