Results 41 to 50 of about 35,698 (247)

Perturbation of maternal PIASy abundance disrupts zygotic genome activation and embryonic development via SUMOylation pathway

Biology Open, 2019
During the maternal-to-zygotic transition (MZT), mRNAs and proteins stored in oocytes are degraded and zygotic genes are activated. We have previously shown that the ubiquitin-proteasome system (UPS)-mediated degradation of maternal proteins plays a role
Chika Higuchi, Mari Yamamoto, Seung-Wook Shin, Kei Miyamoto, Kazuya Matsumoto   +4 more
doaj   +1 more source

A gene-expression screen identifies a non-toxic sumoylation inhibitor that mimics SUMO-less human LRH-1 in liver

eLife, 2015
SUMO-modification of nuclear proteins has profound effects on gene expression. However, non-toxic chemical tools that modulate sumoylation in cells are lacking. Here, to identify small molecule sumoylation inhibitors we developed a cell-based screen that
Miyuki Suzawa, Diego A Miranda, Karmela A Ramos, Kenny K-H Ang, Emily J Faivre, Christopher G Wilson, Laura Caboni, Michelle R Arkin, Yeong-Sang Kim, Robert J Fletterick, Aaron Diaz, John S Schneekloth Jr, Holly A Ingraham   +12 more
doaj   +1 more source

Host SUMOylation in bacterial infections and immune defense mechanisms

Frontiers in Microbiology
SUMOylation, the covalent attachment of small ubiquitin-like modifier proteins (SUMO) to lysine residues of target substrates, has emerged as a crucial post-translational modification regulating various cellular processes.
Yuhua Xu, Xi Ma, Zhifeng Wu, Ruitong Huang, Chenhua Liao, Di Huang, Yujun Tang, Chengbin Zhu, Yaqi Wang, Siyuan Zhang, Peng Liu, Jiaofeng Peng   +11 more
doaj   +1 more source

Post-translational Regulation of GLT-1 in Neurological Diseases and Its Potential as an Effective Therapeutic Target

Frontiers in Molecular Neuroscience, 2019
Glutamate transporter-1 (GLT-1) is a Na+-dependent transporter that plays a key role in glutamate homeostasis by removing excess glutamate in the central nervous system (CNS).
Allison R. Peterson, Devin K. Binder
doaj   +1 more source

mRNA expression analysis of the SUMO pathway genes in the adult mouse retina

Biology Open, 2015
Sumoylation is a reversible post-translational modification that regulates different cellular processes by conjugation/deconjugation of SUMO moieties to target proteins.
Víctor Abad-Morales, Elena B. Domènech, Alejandro Garanto, Gemma Marfany   +3 more
doaj   +1 more source

SUMOylation and bacterial pathogens [PDF]

Virulence, 2010
During infection, bacterial pathogens interfere with many different post-translational modifications of the host cell to promote their own survival and replication. By stimulating or counteracting host post-translational modifications, these pathogens may control locally and specifically the fate and function of host factors critical for the infection ...
David, Ribet, Pascale, Cossart
openaire   +2 more sources

SUMOylation and NEDDylation in kidney diseases

Experimental and Molecular Pathology
Kidney disease poses a serious threat to human health and life, while the lack of specific therapeutic targets hinders the treatment of kidney disease.
Zi-Han Chen, Dan Li, Jian-Yu Zhang, Bo-Yu Wei, Hai-Ling Zhao, Ping Li, Dan-Qian Chen   +6 more
doaj   +1 more source

Dynamic sumoylation of promoter-bound general transcription factors facilitates transcription by RNA polymerase II.

PLoS Genetics, 2021
Transcription-related proteins are frequently identified as targets of sumoylation, including multiple subunits of the RNA polymerase II (RNAPII) general transcription factors (GTFs).
Mohammad S Baig, Yimo Dou, Benjamin G Bergey, Russell Bahar, Justin M Burgener, Marjan Moallem, James B McNeil, Akhi Akhter, Giovanni L Burke, Veroni S Sri Theivakadadcham, Patricia Richard, Damien D'Amours, Emanuel Rosonina   +12 more
doaj   +1 more source

SUMOylation in development and neurodegeneration [PDF]

Development, 2020
ABSTRACT In essentially all eukaryotes, proteins can be modified by the attachment of small ubiquitin-related modifier (SUMO) proteins to lysine side chains to produce branched proteins. This process of ‘SUMOylation’ plays essential roles in plant and animal development by altering protein function in spatially and temporally controlled ...
Tak-Yu Yau, Oscar Molina, Albert J. Courey   +2 more
openaire   +2 more sources

SUMOylation and cell signalling

Biotechnology Journal, 2009
AbstractSUMOylation is a highly transient post‐translational protein modification. Attachment of SUMO to target proteins occurs via a number of specific activating and ligating enzymes that form the SUMO‐substrate complex, and other SUMO‐specific proteases that cleave the covalent bond, thus leaving both SUMO and target protein free for the next round ...
Andreou, Artemisia M., Tavernarakis, Nektarios   +1 more
openaire   +3 more sources