نتایج جستجو برای: sumo1

تعداد نتایج: 347  

Journal: :The Plant cell 2008
Lucio Conti Gillian Price Elizabeth O'Donnell Benjamin Schwessinger Peter Dominy Ari Sadanandom

Understanding salt stress signaling is key to producing salt-tolerant crops. The small ubiquitin-like modifier (SUMO) is a crucial regulator of signaling proteins in eukaryotes. Attachment of SUMO onto substrates is reversible, and SUMO proteases, which specifically cleave the SUMO-substrate linkages, play a vital regulatory role during SUMOylation. We have identified two SUMO proteases, OVERLY...

2014
Xiaodong Sun Jie Li Frederick N. Dong Jin-Tang Dong

ATBF1/ZFHX3 is a large transcription factor that functions in development, tumorigenesis and other biological processes. ATBF1 is normally localized in the nucleus, but is often mislocalized in the cytoplasm in cancer cells. The mechanism underlying the mislocalization of ATBF1 is unknown. In this study, we analyzed the nuclear localization of ATBF1, and found that ectopically expressed ATBF1 f...

2015
Tonghui Yi Shiyu Sun Yibing Huang Yuxin Chen

BACKGROUND Antimicrobial peptides have become important candidates as new antibiotics against resistant bacterial strains. However, the major industrial manufacture of antimicrobial peptides is chemical synthesis with high costs and in relatively small scale. The Ub-tag and SUMO-tag are useful for increasing the yield of enzymes and other proteins in expression system. In this study, antimicrob...

Journal: :Journal of Biological Chemistry 2006

Journal: :Journal of cell science 2007
Rodolfo Zunino Astrid Schauss Peter Rippstein Miguel Andrade-Navarro Heidi M McBride

Mitochondria are dynamic organelles that undergo regulated fission and fusion events that are essential to maintain metabolic stability. We previously demonstrated that the mitochondrial fission GTPase DRP1 is a substrate for SUMOylation. To further understand how SUMOylation impacts mitochondrial function, we searched for a SUMO protease that may affect mitochondrial dynamics. We demonstrate t...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2010
Marcus J Miller Gregory A Barrett-Wilt Zhihua Hua Richard D Vierstra

The covalent attachment of SUMO (small ubiquitin-like modifier) to other intracellular proteins affects a broad range of nuclear processes in yeast and animals, including chromatin maintenance, transcription, and transport across the nuclear envelope, as well as protects proteins from ubiquitin addition. Substantial increases in SUMOylated proteins upon various stresses have also implicated thi...

2018
Hosouk Joung Sehee Kwon Kyoung-Hoon Kim Yun-Gyeong Lee Sera Shin Duk-Hwa Kwon Yeong-Un Lee Taewon Kook Nakwon Choe Jeong Chul Kim Young-Kook Kim Gwang Hyeon Eom Hyun Kook

Sumoylation, the conjugation of a small ubiquitin-like modifier (SUMO) protein to a target, has diverse cellular effects. However, the functional roles of the SUMO modification during myogenesis have not been fully elucidated. Here, we report that basal sumoylation of histone deacetylase 1 (HDAC1) enhances the deacetylation of MyoD in undifferentiated myoblasts, whereas further sumoylation of H...

Journal: :Journal of chemical information and modeling 2013
Ting Shi Yuhui Han Weihua Li Yanlong Zhao Yaqin Liu Zhimin Huang Shaoyong Lu Jian Zhang

The small ubiquitin-related modifier (SUMO)-specific protease (SENP) processes SUMOs to mature forms and deconjugates them from various modified substrates. Loss of the equilibrium from desumoylation catalyzed by abnormal SENP1 is associated with cancers and transcription factor activity. In spite of the significant role of SENP1, the molecular basis of its desumoylation remains unclear. Here, ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2007
Kathrin Kindsmüller Peter Groitl Barbara Härtl Paola Blanchette Joachim Hauber Thomas Dobner

We have investigated the requirements for CRM1-mediated nuclear export and SUMO1 conjugation of the adenovirus E1B-55K protein during productive infection. Our data show that CRM1 is the major export receptor for E1B-55K in infected cells. Functional inactivation of the E1B-55K CRM1-dependent nuclear export signal (NES) or leptomycin B treatment causes an almost complete redistribution of the v...

Journal: :The Biochemical journal 2011
Eva Dütting Nadja Schröder-Kress Heinrich Sticht Ralf Enz

The central nervous system regulates neuronal excitability by macromolecular signalling complexes that consist of functionally related proteins, including neurotransmitter receptors, enzymes and scaffolds. The composition of these signal complexes is regulated by post-translational modifications, such as phosphorylation and SUMOylation (SUMO is small ubiquitin-related modifier). In the present ...

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