The small ubiquitin-related modifier （SUMO） modification plays an important role in the regulation of abscisic acid （ABA） signaling, but the function of the SUMO protease, in ABA signaling, remains largely unknown...The small ubiquitin-related modifier （SUMO） modification plays an important role in the regulation of abscisic acid （ABA） signaling, but the function of the SUMO protease, in ABA signaling, remains largely unknown. Here, we show that the SUMO protease, ASPI positively regulates ABA signaling. Mutations in ASPI resulted in an ABA-insensitive phenotype, during early seedling develop- ment. Wild-type ASP1 successfully rescued, whereas an ASPI mutant （C577S）, defective in SUMO protease activity, failed to rescue, the ABA-insensitive phenotype of asp1-1. Expression of ABI5 and MYB3o target genes was attenuated in asp^-I and our genetic analyses revealed that ASP1 may function upstream of ABI5 and MYB3o.展开更多
Objective: Small ubiquitin-related modifiers (SUMOs) are a group of post-translational modification proteins extensively expressed in eukaryotes. Abnormal SUMOylation can lead to the development of various diseases. T...Objective: Small ubiquitin-related modifiers (SUMOs) are a group of post-translational modification proteins extensively expressed in eukaryotes. Abnormal SUMOylation can lead to the development of various diseases. This article summarizes the progress on research of the role of SUMOs in various types of kidney diseases to further increase the understanding of the regulatory functions of SUMOylation in the pathogenesis of kidney diseases. Data sources: This review was based on articles published in the PubMed databases up to January 2018, using the keywords including "SUMOs," "SUMOylation," and "kidney diseases." Study selection: Original articles and critical reviews about SUMOs and kidney disease were selected for this review. A total of 50 studies were in English. Results: SUMO participates in the activation of NF-κB inflammatory signaling pathway, playing a central regulatory role in the inflammation and progression of DN, and the secretion of various chemokines in AKI. SUMO involves in the regulation of TG2 and Nrf2 antioxidant stress, affecting renal tubular injury in AKI. SUMO affects the MAPK/ERK pathway, regulating intracellular signal transduction, modulating the transcription and expression of effector molecules in DN. SUMO contributes to the TGF-β/Smad pathway, leading to fibrosis of the kidney. The conjugate combination of SUMO and p53 regulates cell proliferation and apoptosis, and participates in the regulation of tumorigenesis. In addition, SUMOylation of MITF modulates renal tumors secondary to melanoma, Similarly, SUMOylation of tumor suppressor gene VHL regulates the occurrence of renal cell carcinoma in VHL syndrome. Conclusions: Tissue injury, inflammatory responses, fibrosis, apoptosis, and tumor proliferation in kidney diseases all involve SUMOs. Further research of the substrate SUMOylation and regulatory mechanisms of SUMO in kidney diseases will improve and develop new treatment measures and strategies targeting kidney diseases.展开更多
Sumoylation is an important protein modification discovered recently. SUMO（small ubiquitin-related modifier） pathway regulates the protein stability and transcriptional activity with a 12-kDa small molecular protein...Sumoylation is an important protein modification discovered recently. SUMO（small ubiquitin-related modifier） pathway regulates the protein stability and transcriptional activity with a 12-kDa small molecular protein, SUMO, ligated to the target protein. The purification of SUMO proteins is a key step to reveal their function. The purpose of this study was to construct the recombinant SUMO1 gene cloned to a pGEX-4T-1 vector to express and purify the SUMO1-GST fusion protein in Escherichia coli. First, the full length DNA sequence of SUMO1 gene was amplified by PCR and was ligated to pMD18-T vector. Then the SUMO1 gene was subcloned to pGEX-4T-1 prokaryotic expression vector between BamHI and XhoI sites, and transformed in Escherichia coli DH5α cells. The right colonies were identified by restrictive enzyme digestion and sequencing. The correct rebombinant plasmid of pGEX-4T-1-SUMO1 was transformed in Escherichia coli BL21 cells and then induced by IPTG（isopropyl- β-D-1- thiogalacto-pyranoside） to express the SUMO1-GST fusion protein. The highly purified SUMO1-GST（glutathione S-transferase） fusion protein was obtained by affinity chromatography. Finally, the properties of SUMO1-GST fusion protein were confirmed by Coomassie brilliant blue strain and Western blot analysis. The recombinant plasmid of pGEX-4T-1-SUMO1 was successfully constructed, and SUMO1-GST fusion proteins were successfully expressed.展开更多
基金Acknowledgments This study was funded by the National Natural Science Foundation of China （81570323, 30972709, 81061120527, 81241082） and the 12th Five-Year National Program of the Ministry of Scientific Technology （2012BAI10B01）. We thank Liu M and Zhou L from Beijing Hospital for providing experimental data, the nurses from Beijing Anzhen Hospital for collecting specimens, and the study volunteers.
文摘编码 adiponectin 受体 1 的基因( ADIPOR1 )和小象ubiquitin一样修饰词( SUMO4 ) 4 被连接了到 anti-atherogenic 效果，但是很少对是否被知道在二基因的多型性，独立行动或交往，没有 diabetes.MethodsWe genotyped ，影响冠的动脉疾病( CAD )的风险没有糖尿病的 200 个 CAD 病人和没有 CAD 的 200 控制，它被选择基于前一个没有 diabetes.ResultsRisk 等位基因，协会也是的潜力在 ADIPOR1 (rs7539542-G， rs7514221-C 和 rs3737884-G ) 在三 SNP 在这些 SNP 和 CAD 的临床的特征之间探索了，没有糖尿病，在在 SUMO4 的 SNP rs237025 的 G 等位基因显著地增加了 CAD 的风险，与从 1.79 ～ 4.44 的 ORs。任何这四风险等位基因的搬运人出现了类似不利 ? 临床的特征。与有 CC 或 GC 遗传型的个人相比，有在 rs3737884 的 GG 遗传型的那些在影响了左前面的下降冠的动脉的 CAD 的显著地更高的风险(或：6.77， P = 0.009 ) ，恰好冠的动脉(或：4.81， P = 0.028 ) 或容器的一个相对大的数字(P = 0.04 ) 。没有糖尿病，在 SUMO4 在 SNP 象风险等位基因一样在 ADIPOR1 在三 SNP 中的至少一个带风险等位基因的个人比不带任何风险等位基因的个人在 CAD 的显著地更高的风险(或：5.82， 95% CI：1.2327.7， P = 0.013 ) 没有糖尿病，在 ADIPOR1 和 SUMO4 的 .ConclusionsSNPs 与 CAD 的提高的风险被联系，并且在二基因的 SNP 可以交往联合影响疾病风险。
基金supported by grants from the National Natural Science Foundation of China(31670186)the Chinese Academy of Sciences(XDA08010105)
文摘The small ubiquitin-related modifier （SUMO） modification plays an important role in the regulation of abscisic acid （ABA） signaling, but the function of the SUMO protease, in ABA signaling, remains largely unknown. Here, we show that the SUMO protease, ASPI positively regulates ABA signaling. Mutations in ASPI resulted in an ABA-insensitive phenotype, during early seedling develop- ment. Wild-type ASP1 successfully rescued, whereas an ASPI mutant （C577S）, defective in SUMO protease activity, failed to rescue, the ABA-insensitive phenotype of asp1-1. Expression of ABI5 and MYB3o target genes was attenuated in asp^-I and our genetic analyses revealed that ASP1 may function upstream of ABI5 and MYB3o.
基金grants from the National Natural Science Foundation of China (No.81870491 and No.81330019)the Major State Basic Research Development Program of China (No.2014CBA02005).
文摘Objective: Small ubiquitin-related modifiers (SUMOs) are a group of post-translational modification proteins extensively expressed in eukaryotes. Abnormal SUMOylation can lead to the development of various diseases. This article summarizes the progress on research of the role of SUMOs in various types of kidney diseases to further increase the understanding of the regulatory functions of SUMOylation in the pathogenesis of kidney diseases. Data sources: This review was based on articles published in the PubMed databases up to January 2018, using the keywords including "SUMOs," "SUMOylation," and "kidney diseases." Study selection: Original articles and critical reviews about SUMOs and kidney disease were selected for this review. A total of 50 studies were in English. Results: SUMO participates in the activation of NF-κB inflammatory signaling pathway, playing a central regulatory role in the inflammation and progression of DN, and the secretion of various chemokines in AKI. SUMO involves in the regulation of TG2 and Nrf2 antioxidant stress, affecting renal tubular injury in AKI. SUMO affects the MAPK/ERK pathway, regulating intracellular signal transduction, modulating the transcription and expression of effector molecules in DN. SUMO contributes to the TGF-β/Smad pathway, leading to fibrosis of the kidney. The conjugate combination of SUMO and p53 regulates cell proliferation and apoptosis, and participates in the regulation of tumorigenesis. In addition, SUMOylation of MITF modulates renal tumors secondary to melanoma, Similarly, SUMOylation of tumor suppressor gene VHL regulates the occurrence of renal cell carcinoma in VHL syndrome. Conclusions: Tissue injury, inflammatory responses, fibrosis, apoptosis, and tumor proliferation in kidney diseases all involve SUMOs. Further research of the substrate SUMOylation and regulatory mechanisms of SUMO in kidney diseases will improve and develop new treatment measures and strategies targeting kidney diseases.
文摘Sumoylation is an important protein modification discovered recently. SUMO（small ubiquitin-related modifier） pathway regulates the protein stability and transcriptional activity with a 12-kDa small molecular protein, SUMO, ligated to the target protein. The purification of SUMO proteins is a key step to reveal their function. The purpose of this study was to construct the recombinant SUMO1 gene cloned to a pGEX-4T-1 vector to express and purify the SUMO1-GST fusion protein in Escherichia coli. First, the full length DNA sequence of SUMO1 gene was amplified by PCR and was ligated to pMD18-T vector. Then the SUMO1 gene was subcloned to pGEX-4T-1 prokaryotic expression vector between BamHI and XhoI sites, and transformed in Escherichia coli DH5α cells. The right colonies were identified by restrictive enzyme digestion and sequencing. The correct rebombinant plasmid of pGEX-4T-1-SUMO1 was transformed in Escherichia coli BL21 cells and then induced by IPTG（isopropyl- β-D-1- thiogalacto-pyranoside） to express the SUMO1-GST fusion protein. The highly purified SUMO1-GST（glutathione S-transferase） fusion protein was obtained by affinity chromatography. Finally, the properties of SUMO1-GST fusion protein were confirmed by Coomassie brilliant blue strain and Western blot analysis. The recombinant plasmid of pGEX-4T-1-SUMO1 was successfully constructed, and SUMO1-GST fusion proteins were successfully expressed.
