Covalent attachment of the small ubiquitin-like modifier (SUMO) to proteins in eukaryotic cells can regulate an assortment of cellular processes including transcription, and DNA-protein and protein-protein interactions. We identified gene models and found evidence for expression of genes involved in SUMOylation and SUMO deconjugation in Populus. We detected SUMOylated proteins in diverse organ and tissue types. SUMOylation was altered during responses to heat shock, desiccation, peroxide and irrigation of roots with high salt solution. SUMO deconjugation from substrates was sensitive to cysteine protease inhibitors. Product sizes and sensitivity to inhibitors are consistent with poly-SUMO chain formation as an intermediate step in SUMO redistribution to substrates in plant cells responding to treatments. The SUMOylation pathway is active in Populus and substrate conjugation to SUMO is a rapid response to multiple inducers.
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http://dx.doi.org/10.1007/s00425-010-1151-8 | DOI Listing |
Clin Genet
January 2025
Prenatal Diagnosis and Fetal Medicine Department, Human Genetics and Genome Research Institute, National Research Centre (NRC), Cairo, Egypt.
SUMOylation involves covalent attachment of small ubiquitin-like modifier (SUMO) proteins to specific lysine residues on target proteins and regulates various aspects of their function. Sentrin-specific proteases (SENPs) are key players in both the conjugation reaction of SUMO proteins to their targets and the subsequent deconjugation of SUMO-conjugated substrates. Here, we provide the first comprehensive prenatal description of a lethal syndrome linked to a novel homozygous stop-gain variant in SENP7 c.
View Article and Find Full Text PDFCancer Lett
December 2024
Shandong Provincial Key Laboratory of Precision Oncology, Shandong Cancer Hospital and Institute, Shandong First Medical University and Shandong Academy of Medical Sciences, Jinan, 250117, China. Electronic address:
Bone marrow stromal cells (BMSCs) are vital for preventing chemotherapy induced apoptosis of multiple myeloma (MM), but roles and machinery in other forms of cell death have not been well elucidated. Here, using an in vitro BMSC-MM interacting model, we observed BMSCs protected MM cells from labile iron pool (LIP) and reactive oxygen species (ROS) triggered ferroptosis by elevating glutathione peroxidase 4 (GPX4). Mechanistically, direct interaction with BMSCs upregulated the expression of SUMO-specific protease 3 (SENP3) in MM cells through CD40/CD40L signaling pathway, and SENP3 de-conjugated SUMO2 at lysine 75 residue to stabilize GPX4 protein, thereby consuming ROS to obviate ferroptosis in MM cells from the Vk∗MYC mouse model, as well as in CD138B220 cells separated from the Cd40l;Prx1 mice (CD40-CKO) and Sumo2 knock out (SUMO2-KO) mice.
View Article and Find Full Text PDFTrends Biochem Sci
December 2024
Institute of Biotechnology and Biomedicine, Autonomous University of Barcelona, 08193 Bellaterra, Spain; Department of Biochemistry and Molecular Biology, Autonomous University of Barcelona, 08193 Bellaterra, Spain. Electronic address:
Ubiquitin (Ub) and ubiquitin-like (UbL) modifications are critical regulators of multiple cellular processes in eukaryotes. These modifications are dynamically controlled by proteases that balance conjugation and deconjugation. In eukaryotes, these proteases include deubiquitinases (DUBs), mostly belonging to the CA-clan of cysteine proteases, and ubiquitin-like proteases (ULPs), belonging to the CE-clan proteases.
View Article and Find Full Text PDFJ Biol Chem
October 2024
College of Life Sciences, Shaanxi Normal University, Xi'an, Shaanxi, China. Electronic address:
Triple-negative breast cancer (TNBC) is a prevalent malignancy in women, casting a formidable shadow on their well-being. Positioned within the nucleolus, SUMO-specific protease 3 (SENP3) assumes a pivotal role in the realms of development and tumorigenesis. However, the participation of SENP3 in TNBC remains a mystery.
View Article and Find Full Text PDFCommun Biol
May 2024
Institut de Biotecnologia i de Biomedicina and Dept. de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193, Bellaterra, Barcelona, Spain.
The post-translational modification of proteins by ubiquitin-like modifiers (UbLs), such as SUMO, ubiquitin, and Nedd8, regulates a vast array of cellular processes. Dedicated UbL deconjugating proteases families reverse these modifications. During bacterial infection, effector proteins, including deconjugating proteases, are released to disrupt host cell defenses and promote bacterial survival.
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