Sumoylation
Small Ubiquitin-Related Modifier Proteins
SUMO-1 Protein
Protein Inhibitors of Activated STAT
Ubiquitin-Conjugating Enzymes
Protein Processing, Post-Translational
Ubiquitin-Protein Ligases
HEK293 Cells
Ubiquitins
Protein Binding
Intranuclear Inclusion Bodies
Ubiquitination
Ubiquitin
COS Cells
Transcription, Genetic
Two-Hybrid System Techniques
HeLa Cells
Amino Acid Motifs
Ubiquitin-Activating Enzymes
Repressor Proteins
Cell Nucleus
Nuclear Proteins
Mutation
Amino Acid Sequence
Cercopithecus aethiops
Transcription Factors
RING Finger Domains
Endopeptidases
Ligases
Protein Structure, Tertiary
Immunoprecipitation
Molecular Sequence Data
Transcriptional Activation
Histone Deacetylases
DNA-Binding Proteins
Protein Transport
Active Transport, Cell Nucleus
Cell Differentiation
Septin2 is modified by SUMOylation and required for chromosome congression in mouse oocytes. (1/424)
In mitosis, centrosomes nucleate microtubules that capture the sister kinetochores of each chromosome to facilitate chromosome congression. In contrast, during meiosis chromosome congression on the acentrosomal spindle is driven primarily by movement of chromosomes along laterally associated microtubule bundles. Previous studies have indicated that septin2 is required for chromosome congression and cytokinesis in mitosis, we therefore asked whether perturbation of septin2 would impair chromosome congression and cytokinesis in meiosis. We have investigated its expression, localization and function during mouse oocyte meiotic maturation. Septin2 was modified by SUMO-1 and its levels remained constant from GVBD to metaphase II stages. Septin2 was localized along the entire spindle at metaphase and at the midbody in cytokinesis. Disruption of septins function with an inhibitor and siRNA caused failure of the metaphase I /anaphase I transition and chromosome misalignment but inhibition of septins after the metaphase I stage did not affect cytokinesis. BubR1, a core component of the spindle checkpoint, was labeled on misaligned chromosomes and on chromosomes aligned at the metaphase plate in inhibitor-treated oocytes that were arrested in prometaphase I/metaphase I, suggesting activation of the spindle assembly checkpoint. Taken together, our results demonstrate that septin2 plays an important role in chromosome congression and meiotic cell cycle progression but not cytokinesis in mouse oocytes. (+info)The SUMO pathway functions in mouse oocyte maturation. (2/424)
Sumoylation is an important post-translational modification in which SUMO (small ubiquitin-related modifier) proteins are bonded covalently to their substrates. Studies on the roles of sumoylation in cell cycle regulation have been emerging in both mitosis from yeast to mammals and meiosis in budding yeast, but the functions of sumoylation in mammalian meiosis, especially in oocyte meiotic maturation are not well known. Here, we examined the localization and expression of SUMO-1 and SUMO-2/3, the two basic proteins in the sumoylation pathway and investigated their roles through over-expression of Senp2 during mouse oocyte maturation. Immunofluorescent staining revealed differential patterns of SUMO-1 and SUMO-2/3 localization: SUMO-1 was localized to the spindle poles in prometaphase I, MI and MII stages, around the separating homologues in anaphase I and telophase I stages of first meiosis, while SUMO-2/3 was mainly concentrated near centromeres during mouse oocyte maturation. Immunoblot analysis uncovered the different expression profiles of SUMO-1 and SUMO-2/3 modified proteins during mouse oocyte maturation. Over-expression of Senp2, a SUMO-specific isopeptidase, caused changes of SUMO-modified proteins and led to defects in MII spindle organization in mature eggs. These results suggest that the SUMO pathway may play an indispensable role during mouse oocyte meiotic maturation. (+info)SIRT1 stabilizes PML promoting its sumoylation. (3/424)
(+info)SUMOylation modulates the function of Aurora-B kinase. (4/424)
(+info)Glucocorticoid-induced activation of caspase-8 protects the glucocorticoid-induced protein Gilz from proteasomal degradation and induces its binding to SUMO-1 in murine thymocytes. (5/424)
(+info)Rod/Zw10 complex is required for PIASy-dependent centromeric SUMOylation. (6/424)
(+info)Resistance to rabies virus infection conferred by the PMLIV isoform. (7/424)
(+info)The fate of metaphase kinetochores is weighed in the balance of SUMOylation during S phase. (8/424)
(+info)Sumoylation is a post-translational modification process in which a small ubiquitin-like modifier (SUMO) protein is covalently attached to specific lysine residues on target proteins. This conjugation is facilitated by an enzymatic cascade involving E1 activating enzyme, E2 conjugating enzyme, and E3 ligase. Sumoylation can regulate various cellular functions such as protein stability, subcellular localization, activity, and interaction with other proteins. It plays crucial roles in numerous biological processes including DNA replication, repair, transcription, and chromatin remodeling, as well as stress response and regulation of the cell cycle. Dysregulation of sumoylation has been implicated in various human diseases, such as cancer, neurodegenerative disorders, and viral infections.
Small Ubiquitin-Related Modifier (SUMO) proteins are a type of post-translational modifier, similar to ubiquitin, that can be covalently attached to other proteins in a process called sumoylation. This modification plays a crucial role in regulating various cellular processes such as nuclear transport, transcriptional regulation, DNA repair, and protein stability. Sumoylation is a dynamic and reversible process, which allows for precise control of these functions under different physiological conditions.
The human genome encodes four SUMO paralogs (SUMO1-4), among which SUMO2 and SUMO3 share 97% sequence identity and are often referred to as a single entity, SUMO2/3. The fourth member, SUMO4, is less conserved and has a more restricted expression pattern compared to the other three paralogs.
Similar to ubiquitination, sumoylation involves an enzymatic cascade consisting of an E1 activating enzyme (SAE1/UBA2 heterodimer), an E2 conjugating enzyme (UBC9), and an E3 ligase that facilitates the transfer of SUMO from the E2 to the target protein. The process can be reversed by SUMO-specific proteases, which cleave the isopeptide bond between the modified lysine residue on the target protein and the C-terminal glycine of the SUMO molecule.
Dysregulation of sumoylation has been implicated in various human diseases, including cancer, neurodegenerative disorders, and viral infections. Therefore, understanding the molecular mechanisms governing this post-translational modification is essential for developing novel therapeutic strategies targeting these conditions.
SUMO-1 (Small Ubiquitin-like Modifier 1) protein is a member of the SUMO family of post-translational modifiers, which are involved in the regulation of various cellular processes such as nuclear-cytoplasmic transport, transcriptional regulation, and DNA repair. The SUMO-1 protein is covalently attached to specific lysine residues on target proteins through a process called sumoylation, which can alter the activity, localization, or stability of the modified protein. Sumoylation plays a crucial role in maintaining cellular homeostasis and has been implicated in several human diseases, including cancer and neurodegenerative disorders.
Protein Inhibitors of Activated STAT (PIAS) are a family of proteins that regulate the activity of signal transducer and activator of transcription (STAT) proteins, which are involved in various cellular processes such as differentiation, proliferation, and apoptosis. PIAS proteins function as E3 ubiquitin ligases and SUMO (small ubiquitin-like modifier) ligases, modifying STAT proteins and other transcription factors by adding SUMO molecules to them. This modification can alter the activity, localization, or stability of the target protein, thereby regulating its function in the cell. PIAS proteins have been shown to play a role in various physiological and pathological processes, including inflammation, cancer, and neurodegenerative diseases. Inhibiting PIAS proteins has emerged as a potential therapeutic strategy for the treatment of certain diseases associated with aberrant STAT activation.
Ubiquitin-conjugating enzymes (UBCs or E2 enzymes) are a family of enzymes that play a crucial role in the ubiquitination process, which is a post-translational modification of proteins. This process involves the covalent attachment of the protein ubiquitin to specific lysine residues on target proteins, ultimately leading to their degradation by the 26S proteasome.
Ubiquitination is a multi-step process that requires the coordinated action of three types of enzymes: E1 (ubiquitin-activating), E2 (ubiquitin-conjugating), and E3 (ubiquitin ligases). Ubiquitin-conjugating enzymes are responsible for transferring ubiquitin from the E1 enzyme to the target protein, which is facilitated by an E3 ubiquitin ligase. The human genome encodes around 40 different UBCs, each with unique substrate specificities and functions in various cellular processes, such as protein degradation, DNA repair, and signal transduction.
Ubiquitination is a highly regulated process that can be reversed by the action of deubiquitinating enzymes (DUBs), which remove ubiquitin molecules from target proteins. Dysregulation of the ubiquitination pathway has been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions.
Lysine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. Its chemical formula is (2S)-2,6-diaminohexanoic acid. Lysine is necessary for the growth and maintenance of tissues in the body, and it plays a crucial role in the production of enzymes, hormones, and antibodies. It is also essential for the absorption of calcium and the formation of collagen, which is an important component of bones and connective tissue. Foods that are good sources of lysine include meat, poultry, fish, eggs, and dairy products.
Post-translational protein processing refers to the modifications and changes that proteins undergo after their synthesis on ribosomes, which are complex molecular machines responsible for protein synthesis. These modifications occur through various biochemical processes and play a crucial role in determining the final structure, function, and stability of the protein.
The process begins with the translation of messenger RNA (mRNA) into a linear polypeptide chain, which is then subjected to several post-translational modifications. These modifications can include:
1. Proteolytic cleavage: The removal of specific segments or domains from the polypeptide chain by proteases, resulting in the formation of mature, functional protein subunits.
2. Chemical modifications: Addition or modification of chemical groups to the side chains of amino acids, such as phosphorylation (addition of a phosphate group), glycosylation (addition of sugar moieties), methylation (addition of a methyl group), acetylation (addition of an acetyl group), and ubiquitination (addition of a ubiquitin protein).
3. Disulfide bond formation: The oxidation of specific cysteine residues within the polypeptide chain, leading to the formation of disulfide bonds between them. This process helps stabilize the three-dimensional structure of proteins, particularly in extracellular environments.
4. Folding and assembly: The acquisition of a specific three-dimensional conformation by the polypeptide chain, which is essential for its function. Chaperone proteins assist in this process to ensure proper folding and prevent aggregation.
5. Protein targeting: The directed transport of proteins to their appropriate cellular locations, such as the nucleus, mitochondria, endoplasmic reticulum, or plasma membrane. This is often facilitated by specific signal sequences within the protein that are recognized and bound by transport machinery.
Collectively, these post-translational modifications contribute to the functional diversity of proteins in living organisms, allowing them to perform a wide range of cellular processes, including signaling, catalysis, regulation, and structural support.
Ubiquitin-protein ligases, also known as E3 ubiquitin ligases, are a group of enzymes that play a crucial role in the ubiquitination process. Ubiquitination is a post-translational modification where ubiquitin molecules are attached to specific target proteins, marking them for degradation by the proteasome or for other regulatory functions.
Ubiquitin-protein ligases catalyze the final step in this process by binding to both the ubiquitin protein and the target protein, facilitating the transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to the target protein. There are several different types of ubiquitin-protein ligases, each with their own specificity for particular target proteins and regulatory functions.
Ubiquitin-protein ligases have been implicated in various cellular processes such as protein degradation, DNA repair, signal transduction, and regulation of the cell cycle. Dysregulation of ubiquitination has been associated with several diseases, including cancer, neurodegenerative disorders, and inflammatory responses. Therefore, understanding the function and regulation of ubiquitin-protein ligases is an important area of research in biology and medicine.
HEK293 cells, also known as human embryonic kidney 293 cells, are a line of cells used in scientific research. They were originally derived from human embryonic kidney cells and have been adapted to grow in a lab setting. HEK293 cells are widely used in molecular biology and biochemistry because they can be easily transfected (a process by which DNA is introduced into cells) and highly express foreign genes. As a result, they are often used to produce proteins for structural and functional studies. It's important to note that while HEK293 cells are derived from human tissue, they have been grown in the lab for many generations and do not retain the characteristics of the original embryonic kidney cells.
Ubiquitin is a small protein that is present in most tissues in the body. It plays a critical role in regulating many important cellular processes, such as protein degradation and DNA repair. Ubiquitin can attach to other proteins in a process called ubiquitination, which can target the protein for degradation or modify its function.
Ubiquitination involves a series of enzymatic reactions that ultimately result in the attachment of ubiquitin molecules to specific lysine residues on the target protein. The addition of a single ubiquitin molecule is called monoubiquitination, while the addition of multiple ubiquitin molecules is called polyubiquitination.
Polyubiquitination can serve as a signal for proteasomal degradation, where the target protein is broken down into its component amino acids by the 26S proteasome complex. Monoubiquitination and other forms of ubiquitination can also regulate various cellular processes, such as endocytosis, DNA repair, and gene expression.
Dysregulation of ubiquitin-mediated protein degradation has been implicated in a variety of diseases, including cancer, neurodegenerative disorders, and inflammatory conditions.
Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.
In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.
Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.
Intranuclear inclusion bodies are abnormal, rounded structures found within the nucleus of a cell. They are composed of aggregated proteins or other cellular components and can be associated with various viral infections and certain genetic disorders. These inclusion bodies can interfere with normal nuclear functions, leading to cell damage and contributing to the pathogenesis of diseases such as cytomegalovirus infection, rabies, and some forms of neurodegenerative disorders like polyglutamine diseases. The presence of intranuclear inclusion bodies is often used in diagnostic pathology to help identify specific underlying conditions.
Ubiquitination is a post-translational modification process in which a ubiquitin protein is covalently attached to a target protein. This process plays a crucial role in regulating various cellular functions, including protein degradation, DNA repair, and signal transduction. The addition of ubiquitin can lead to different outcomes depending on the number and location of ubiquitin molecules attached to the target protein. Monoubiquitination (the attachment of a single ubiquitin molecule) or multiubiquitination (the attachment of multiple ubiquitin molecules) can mark proteins for degradation by the 26S proteasome, while specific types of ubiquitination (e.g., K63-linked polyubiquitination) can serve as a signal for nonproteolytic functions such as endocytosis, autophagy, or DNA repair. Ubiquitination is a highly regulated process that involves the coordinated action of three enzymes: E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme, and E3 ubiquitin ligase. Dysregulation of ubiquitination has been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions.
Ubiquitin is a small protein that is present in all eukaryotic cells and plays a crucial role in the regulation of various cellular processes, such as protein degradation, DNA repair, and stress response. It is involved in marking proteins for destruction by attaching to them, a process known as ubiquitination. This modification can target proteins for degradation by the proteasome, a large protein complex that breaks down unneeded or damaged proteins in the cell. Ubiquitin also has other functions, such as regulating the localization and activity of certain proteins. The ability of ubiquitin to modify many different proteins and play a role in multiple cellular processes makes it an essential player in maintaining cellular homeostasis.
COS cells are a type of cell line that are commonly used in molecular biology and genetic research. The name "COS" is an acronym for "CV-1 in Origin," as these cells were originally derived from the African green monkey kidney cell line CV-1. COS cells have been modified through genetic engineering to express high levels of a protein called SV40 large T antigen, which allows them to efficiently take up and replicate exogenous DNA.
There are several different types of COS cells that are commonly used in research, including COS-1, COS-3, and COS-7 cells. These cells are widely used for the production of recombinant proteins, as well as for studies of gene expression, protein localization, and signal transduction.
It is important to note that while COS cells have been a valuable tool in scientific research, they are not without their limitations. For example, because they are derived from monkey kidney cells, there may be differences in the way that human genes are expressed or regulated in these cells compared to human cells. Additionally, because COS cells express SV40 large T antigen, they may have altered cell cycle regulation and other phenotypic changes that could affect experimental results. Therefore, it is important to carefully consider the choice of cell line when designing experiments and interpreting results.
Genetic transcription is the process by which the information in a strand of DNA is used to create a complementary RNA molecule. This process is the first step in gene expression, where the genetic code in DNA is converted into a form that can be used to produce proteins or functional RNAs.
During transcription, an enzyme called RNA polymerase binds to the DNA template strand and reads the sequence of nucleotide bases. As it moves along the template, it adds complementary RNA nucleotides to the growing RNA chain, creating a single-stranded RNA molecule that is complementary to the DNA template strand. Once transcription is complete, the RNA molecule may undergo further processing before it can be translated into protein or perform its functional role in the cell.
Transcription can be either "constitutive" or "regulated." Constitutive transcription occurs at a relatively constant rate and produces essential proteins that are required for basic cellular functions. Regulated transcription, on the other hand, is subject to control by various intracellular and extracellular signals, allowing cells to respond to changing environmental conditions or developmental cues.
A two-hybrid system technique is a type of genetic screening method used in molecular biology to identify protein-protein interactions within an organism, most commonly baker's yeast (Saccharomyces cerevisiae) or Escherichia coli. The name "two-hybrid" refers to the fact that two separate proteins are being examined for their ability to interact with each other.
The technique is based on the modular nature of transcription factors, which typically consist of two distinct domains: a DNA-binding domain (DBD) and an activation domain (AD). In a two-hybrid system, one protein of interest is fused to the DBD, while the second protein of interest is fused to the AD. If the two proteins interact, the DBD and AD are brought in close proximity, allowing for transcriptional activation of a reporter gene that is linked to a specific promoter sequence recognized by the DBD.
The main components of a two-hybrid system include:
1. Bait protein (fused to the DNA-binding domain)
2. Prey protein (fused to the activation domain)
3. Reporter gene (transcribed upon interaction between bait and prey proteins)
4. Promoter sequence (recognized by the DBD when brought in proximity due to interaction)
The two-hybrid system technique has several advantages, including:
1. Ability to screen large libraries of potential interacting partners
2. High sensitivity for detecting weak or transient interactions
3. Applicability to various organisms and protein types
4. Potential for high-throughput analysis
However, there are also limitations to the technique, such as false positives (interactions that do not occur in vivo) and false negatives (lack of detection of true interactions). Additionally, the fusion proteins may not always fold or localize correctly, leading to potential artifacts. Despite these limitations, two-hybrid system techniques remain a valuable tool for studying protein-protein interactions and have contributed significantly to our understanding of various cellular processes.
A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.
HeLa cells are a type of immortalized cell line used in scientific research. They are derived from a cancer that developed in the cervical tissue of Henrietta Lacks, an African-American woman, in 1951. After her death, cells taken from her tumor were found to be capable of continuous division and growth in a laboratory setting, making them an invaluable resource for medical research.
HeLa cells have been used in a wide range of scientific studies, including research on cancer, viruses, genetics, and drug development. They were the first human cell line to be successfully cloned and are able to grow rapidly in culture, doubling their population every 20-24 hours. This has made them an essential tool for many areas of biomedical research.
It is important to note that while HeLa cells have been instrumental in numerous scientific breakthroughs, the story of their origin raises ethical questions about informed consent and the use of human tissue in research.
Amino acid motifs are recurring patterns or sequences of amino acids in a protein molecule. These motifs can be identified through various sequence analysis techniques and often have functional or structural significance. They can be as short as two amino acids in length, but typically contain at least three to five residues.
Some common examples of amino acid motifs include:
1. Active site motifs: These are specific sequences of amino acids that form the active site of an enzyme and participate in catalyzing chemical reactions. For example, the catalytic triad in serine proteases consists of three residues (serine, histidine, and aspartate) that work together to hydrolyze peptide bonds.
2. Signal peptide motifs: These are sequences of amino acids that target proteins for secretion or localization to specific organelles within the cell. For example, a typical signal peptide consists of a positively charged n-region, a hydrophobic h-region, and a polar c-region that directs the protein to the endoplasmic reticulum membrane for translocation.
3. Zinc finger motifs: These are structural domains that contain conserved sequences of amino acids that bind zinc ions and play important roles in DNA recognition and regulation of gene expression.
4. Transmembrane motifs: These are sequences of hydrophobic amino acids that span the lipid bilayer of cell membranes and anchor transmembrane proteins in place.
5. Phosphorylation sites: These are specific serine, threonine, or tyrosine residues that can be phosphorylated by protein kinases to regulate protein function.
Understanding amino acid motifs is important for predicting protein structure and function, as well as for identifying potential drug targets in disease-associated proteins.
Ubiquitin-activating enzymes, also known as E1 enzymes, are a class of enzymes that play a crucial role in the ubiquitination pathway. Ubiquitination is a post-translational modification process that targets proteins for degradation or regulates their function by attaching a small protein called ubiquitin to them.
E1 enzymes initiate the ubiquitination process by activating ubiquitin through a two-step reaction. First, they catalyze the adenylation of ubiquitin's carboxyl terminus using ATP as an energy source, forming an adenylated ubiquitin intermediate. Then, the E1 enzyme transfers the activated ubiquitin to a cysteine residue on its own active site, forming a thioester bond between the ubiquitin and the E1 enzyme.
After activation, ubiquitin is transferred from the E1 enzyme to an E2 ubiquitin-conjugating enzyme, which then works with an E3 ubiquitin ligase to transfer ubiquitin to a specific lysine residue on the target protein. The addition of multiple ubiquitin molecules can create a polyubiquitin chain, leading to proteasomal degradation or other functional changes in the targeted protein.
There are two main families of E1 enzymes: UBA1 and UBA6. Dysregulation of ubiquitination pathways has been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions. Therefore, understanding the function and regulation of E1 enzymes is essential for developing potential therapeutic strategies targeting these pathways.
Repressor proteins are a type of regulatory protein in molecular biology that suppress the transcription of specific genes into messenger RNA (mRNA) by binding to DNA. They function as part of gene regulation processes, often working in conjunction with an operator region and a promoter region within the DNA molecule. Repressor proteins can be activated or deactivated by various signals, allowing for precise control over gene expression in response to changing cellular conditions.
There are two main types of repressor proteins:
1. DNA-binding repressors: These directly bind to specific DNA sequences (operator regions) near the target gene and prevent RNA polymerase from transcribing the gene into mRNA.
2. Allosteric repressors: These bind to effector molecules, which then cause a conformational change in the repressor protein, enabling it to bind to DNA and inhibit transcription.
Repressor proteins play crucial roles in various biological processes, such as development, metabolism, and stress response, by controlling gene expression patterns in cells.
The cell nucleus is a membrane-bound organelle found in the eukaryotic cells (cells with a true nucleus). It contains most of the cell's genetic material, organized as DNA molecules in complex with proteins, RNA molecules, and histones to form chromosomes.
The primary function of the cell nucleus is to regulate and control the activities of the cell, including growth, metabolism, protein synthesis, and reproduction. It also plays a crucial role in the process of mitosis (cell division) by separating and protecting the genetic material during this process. The nuclear membrane, or nuclear envelope, surrounding the nucleus is composed of two lipid bilayers with numerous pores that allow for the selective transport of molecules between the nucleoplasm (nucleus interior) and the cytoplasm (cell exterior).
The cell nucleus is a vital structure in eukaryotic cells, and its dysfunction can lead to various diseases, including cancer and genetic disorders.
Nuclear proteins are a category of proteins that are primarily found in the nucleus of a eukaryotic cell. They play crucial roles in various nuclear functions, such as DNA replication, transcription, repair, and RNA processing. This group includes structural proteins like lamins, which form the nuclear lamina, and regulatory proteins, such as histones and transcription factors, that are involved in gene expression. Nuclear localization signals (NLS) often help target these proteins to the nucleus by interacting with importin proteins during active transport across the nuclear membrane.
A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
'Cercopithecus aethiops' is the scientific name for the monkey species more commonly known as the green monkey. It belongs to the family Cercopithecidae and is native to western Africa. The green monkey is omnivorous, with a diet that includes fruits, nuts, seeds, insects, and small vertebrates. They are known for their distinctive greenish-brown fur and long tail. Green monkeys are also important animal models in biomedical research due to their susceptibility to certain diseases, such as SIV (simian immunodeficiency virus), which is closely related to HIV.
Transcription factors are proteins that play a crucial role in regulating gene expression by controlling the transcription of DNA to messenger RNA (mRNA). They function by binding to specific DNA sequences, known as response elements, located in the promoter region or enhancer regions of target genes. This binding can either activate or repress the initiation of transcription, depending on the properties and interactions of the particular transcription factor. Transcription factors often act as part of a complex network of regulatory proteins that determine the precise spatiotemporal patterns of gene expression during development, differentiation, and homeostasis in an organism.
Ring finger domains (RFIDs) are a type of protein domain that contain a characteristic cysteine-rich motif. They were initially identified in the RAS-associated proteins called Ras GTPase-activating proteins (GAPs), where they are involved in mediating protein-protein interactions.
The name "ring finger" comes from the fact that these domains contain a series of cysteine and histidine residues that coordinate a central zinc ion, forming a structural ring. This ring is thought to play a role in stabilizing the overall structure of the domain and facilitating its interactions with other proteins.
RFIDs are found in a wide variety of proteins, including transcription factors, chromatin modifiers, and signaling molecules. They have been implicated in a range of cellular processes, including transcriptional regulation, DNA repair, and signal transduction. Mutations in RFID-containing proteins have been linked to various human diseases, including cancer and neurological disorders.
Endopeptidases are a type of enzyme that breaks down proteins by cleaving peptide bonds inside the polypeptide chain. They are also known as proteinases or endoproteinases. These enzymes work within the interior of the protein molecule, cutting it at specific points along its length, as opposed to exopeptidases, which remove individual amino acids from the ends of the protein chain.
Endopeptidases play a crucial role in various biological processes, such as digestion, blood coagulation, and programmed cell death (apoptosis). They are classified based on their catalytic mechanism and the structure of their active site. Some examples of endopeptidase families include serine proteases, cysteine proteases, aspartic proteases, and metalloproteases.
It is important to note that while endopeptidases are essential for normal physiological functions, they can also contribute to disease processes when their activity is unregulated or misdirected. For instance, excessive endopeptidase activity has been implicated in the pathogenesis of neurodegenerative disorders, cancer, and inflammatory conditions.
Ligases are a group of enzymes that catalyze the formation of a covalent bond between two molecules, usually involving the joining of two nucleotides in a DNA or RNA strand. They play a crucial role in various biological processes such as DNA replication, repair, and recombination. In DNA ligases, the enzyme seals nicks or breaks in the phosphodiester backbone of the DNA molecule by catalyzing the formation of an ester bond between the 3'-hydroxyl group and the 5'-phosphate group of adjacent nucleotides. This process is essential for maintaining genomic integrity and stability.
Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.
Immunoprecipitation (IP) is a research technique used in molecular biology and immunology to isolate specific antigens or antibodies from a mixture. It involves the use of an antibody that recognizes and binds to a specific antigen, which is then precipitated out of solution using various methods, such as centrifugation or chemical cross-linking.
In this technique, an antibody is first incubated with a sample containing the antigen of interest. The antibody specifically binds to the antigen, forming an immune complex. This complex can then be captured by adding protein A or G agarose beads, which bind to the constant region of the antibody. The beads are then washed to remove any unbound proteins, leaving behind the precipitated antigen-antibody complex.
Immunoprecipitation is a powerful tool for studying protein-protein interactions, post-translational modifications, and signal transduction pathways. It can also be used to detect and quantify specific proteins in biological samples, such as cells or tissues, and to identify potential biomarkers of disease.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
Transcriptional activation is the process by which a cell increases the rate of transcription of specific genes from DNA to RNA. This process is tightly regulated and plays a crucial role in various biological processes, including development, differentiation, and response to environmental stimuli.
Transcriptional activation occurs when transcription factors (proteins that bind to specific DNA sequences) interact with the promoter region of a gene and recruit co-activator proteins. These co-activators help to remodel the chromatin structure around the gene, making it more accessible for the transcription machinery to bind and initiate transcription.
Transcriptional activation can be regulated at multiple levels, including the availability and activity of transcription factors, the modification of histone proteins, and the recruitment of co-activators or co-repressors. Dysregulation of transcriptional activation has been implicated in various diseases, including cancer and genetic disorders.
The intranuclear space, also known as the nucleoplasm or karyolymph, refers to the internal environment of a eukaryotic cell's nucleus. It is the fluid-filled space inside the nuclear membrane where the genetic material, chromatin, and various nuclear organelles such as the nucleolus are suspended. The intranuclear space is involved in numerous essential cellular processes, including DNA replication, transcription, and repair.
Histone deacetylases (HDACs) are a group of enzymes that play a crucial role in the regulation of gene expression. They work by removing acetyl groups from histone proteins, which are the structural components around which DNA is wound to form chromatin, the material that makes up chromosomes.
Histone acetylation is a modification that generally results in an "open" chromatin structure, allowing for the transcription of genes into proteins. When HDACs remove these acetyl groups, the chromatin becomes more compact and gene expression is reduced or silenced.
HDACs are involved in various cellular processes, including development, differentiation, and survival. Dysregulation of HDAC activity has been implicated in several diseases, such as cancer, neurodegenerative disorders, and cardiovascular diseases. As a result, HDAC inhibitors have emerged as promising therapeutic agents for these conditions.
DNA-binding proteins are a type of protein that have the ability to bind to DNA (deoxyribonucleic acid), the genetic material of organisms. These proteins play crucial roles in various biological processes, such as regulation of gene expression, DNA replication, repair and recombination.
The binding of DNA-binding proteins to specific DNA sequences is mediated by non-covalent interactions, including electrostatic, hydrogen bonding, and van der Waals forces. The specificity of binding is determined by the recognition of particular nucleotide sequences or structural features of the DNA molecule.
DNA-binding proteins can be classified into several categories based on their structure and function, such as transcription factors, histones, and restriction enzymes. Transcription factors are a major class of DNA-binding proteins that regulate gene expression by binding to specific DNA sequences in the promoter region of genes and recruiting other proteins to modulate transcription. Histones are DNA-binding proteins that package DNA into nucleosomes, the basic unit of chromatin structure. Restriction enzymes are DNA-binding proteins that recognize and cleave specific DNA sequences, and are widely used in molecular biology research and biotechnology applications.
Protein transport, in the context of cellular biology, refers to the process by which proteins are actively moved from one location to another within or between cells. This is a crucial mechanism for maintaining proper cell function and regulation.
Intracellular protein transport involves the movement of proteins within a single cell. Proteins can be transported across membranes (such as the nuclear envelope, endoplasmic reticulum, Golgi apparatus, or plasma membrane) via specialized transport systems like vesicles and transport channels.
Intercellular protein transport refers to the movement of proteins from one cell to another, often facilitated by exocytosis (release of proteins in vesicles) and endocytosis (uptake of extracellular substances via membrane-bound vesicles). This is essential for communication between cells, immune response, and other physiological processes.
It's important to note that any disruption in protein transport can lead to various diseases, including neurological disorders, cancer, and metabolic conditions.
I'm sorry for any confusion, but "Active Transport, Cell Nucleus" is not a widely recognized or established medical term. Active transport typically refers to the energy-dependent process by which cells move molecules across their membranes against their concentration gradient. This process is facilitated by transport proteins and requires ATP as an energy source. However, this process primarily occurs in the cell membrane and not in the cell nucleus.
The cell nucleus, on the other hand, contains genetic material (DNA) and is responsible for controlling various cellular activities such as gene expression, replication, and repair. While there are transport processes that occur within the nucleus, they do not typically involve active transport in the same way that it occurs at the cell membrane.
Therefore, a medical definition of "Active Transport, Cell Nucleus" would not be applicable or informative in this context.
Cell differentiation is the process by which a less specialized cell, or stem cell, becomes a more specialized cell type with specific functions and structures. This process involves changes in gene expression, which are regulated by various intracellular signaling pathways and transcription factors. Differentiation results in the development of distinct cell types that make up tissues and organs in multicellular organisms. It is a crucial aspect of embryonic development, tissue repair, and maintenance of homeostasis in the body.
The crystalline lens is a biconvex transparent structure in the eye that helps to refract (bend) light rays and focus them onto the retina. It is located behind the iris and pupil and is suspended by small fibers called zonules that connect it to the ciliary body. The lens can change its shape to accommodate and focus on objects at different distances, a process known as accommodation. With age, the lens may become cloudy or opaque, leading to cataracts.
ABHD18
Protein inhibitor of activated STAT
Actin
TMEM221
Tetratricopeptide repeat protein 39B
C17orf98
UBE2I
C4orf45
C11orf98
SUHW4
UBA2
Transmembrane protein 251
IFFO1
RANGAP1
PRR16
DACH1
Ubiquitin-like protein
SUMO1
WD Repeat and Coiled Coil Containing Protein
Zinc finger protein 800
Histone-modifying enzymes
Stress granule
Histone code
Lysine
TMEM39B
HIST4H4
C20orf27
SBK3
C1orf112
Eduardo Arzt
Sumoylation and Aging - Research Projects - Samuelson Lab - University of Rochester Medical Center
Viruses | Free Full-Text | Human SUMOylation Pathway Is Critical for Influenza B Virus
Frontiers | Regulation of SUMOylation Targets Associated With Wnt/β-Catenin Pathway
Cell Lines For Studying Sumoylation
Cell Lines For Studying Sumoylation
Mitotic SUMOylation: Unraveling the role of DNA Topoisomerase IIα SUMOylation and PIASy SUMO E3 ligase in mitosis
Senp2 regulates adipose lipid storage by de-SUMOylation of Setdb1, Journal of Molecular Cell Biology | 10.1093/jmcb/mjx055 |...
SUMOylation of Bonus, the Drosophila homolog of Transcription Intermediary Factor 1, safeguards germline identity by recruiting...
Interplay between SUMOylation and NEDDylation regulates RPL11 localization and function<...
The Next Frontier: Translational Development of Ubiquitination, SUMOylation, and NEDDylation in Cancer. - Nuffield Department...
Lung neuroendocrine tumors: correlation of ubiquitinylation and sumoylation with nucleo-cytosolic partitioning of PTEN | BMC...
Frontiers | Hacker within! Ehrlichia chaffeensis Effector Driven Phagocyte Reprogramming Strategy
EpiQuik In Vivo Universal Protein Sumoylation Assay Kit | EpigenTek
Sumoylation differentially regulates Sp1 to control cell differentiation<...
PPARγ sumoylation-mediated lipid accumulation in lung cancer | Oncotarget
ABHD18 - Wikipedia
NOTCH1 activation in breast cancer confers sensitivity to inhibition of SUMOylation - Ludwig Cancer Research
EN (en)
SUMOylation and DeSUMOylation: Prospective therapeutic targets in cancer. | Life Sci;332: 122085, 2023 Nov 01. | MEDLINE
UHRF2 ubiquitin like with PHD and ring finger domains 2 [Homo sapiens (human)] - Gene - NCBI
People - The University of Nottingham
KEPE--a motif frequently superimposed on sumoylation sites in metazoan chromatin proteins and transcription factors. -...
SUMOylation Is Required for Glycine-Induced Increases in AMPA Receptor Surface Expression (ChemLTP) in Hippocampal Neurons<...
Ginkgolic acid (GA) was chosen to suppress the sumoylation pathway because it was reported like a potent inhibitor of the...
Nonsynonymous Single-Nucleotide Variations on Some Posttranslational Modifications of Human Proteins and the Association with...
Ion (eleven, 12). Modest ubiquitin-related modifier 77337-73-6 References proteins (SUMOs) may be covalently conjugated ...
Research, Abe Lab | MD Anderson Cancer Center
Recombinant Human KAP1 protein (denatured) (ab171679) | Abcam
Key mechanism in the plant defense against fungal infections | ScienceDaily
O-GlcNAcylation of STAT5 controls tyrosine phosphorylation and oncogenic transcription in STAT5-dependent malignancies |...
Proteins21
- SUMOylation is a post-translational modification of proteins that has been found to play a major role in the Wnt/β-catenin signaling pathway. (frontiersin.org)
- Post-translational modifications (PTMs) of proteins, including phosphorylation, acetylation, ubiquitination, and SUMOylation, can regulate the function of proteins, determine the active state and subcellular location of proteins, and dynamically interact with other proteins related to carcinogenesis and progression ( 17 - 20 ). (frontiersin.org)
- SUMOylation of proteins is an important mechanism in cellular responses to environmental stress ( 21 , 22 ). (frontiersin.org)
- Proteins associated with the Wnt/β-catenin pathway have been identified as SUMOylated substrates, and evidences suggested that the initiation and progression of cancers depended on the function of the SUMOylation ( 23 ). (frontiersin.org)
- Our group has identified DNA topoisomerase IIα (Topo IIα) as one of the important mitotic proteins for SUMOylation. (ku.edu)
- Finally, we showed that Bonus SUMOylation is mediated by the SUMO E3-ligase Su(var)2-10, revealing that although SUMOylation of TIF1 proteins is conserved between insects and mammals, both the mechanism and specific site of modification is different in the two taxa. (elifesciences.org)
- Flexible antibody choice allows the detection of sumoylation of multiple target proteins simultaneously. (epigentek.com)
- The EpiQuik™ In Vivo Universal Protein Sumoylation Assay Kit is designed for measuring sumoylation of targeted proteins. (epigentek.com)
- Sumoylation of the targeted proteins is indicated by SUMO conjugated to these proteins. (epigentek.com)
- Sumoylation of the targeted proteins is detected by recognition of SUMO conjugated to these proteins with an anti-SUMO antibody. (epigentek.com)
- In yeast, septins were among the first proteins reported to be modified by SUMOylation, a ubiquitin-like posttranslational modification. (pasteur.fr)
- However, polyubiquitination can lead to the degradation of substrate proteins , while poly- SUMOylation only leads to the degradation of substrate proteins through the proteasome pathway after being recognized by ubiquitin as a signal factor. (bvsalud.org)
- The SUMOylation modification system affects the localization , activation and turnover of proteins in cells and participates in regulating most nuclear and extranuclear molecular reactions. (bvsalud.org)
- Abnormal expression of proteins related to the SUMOylation pathway is commonly observed in tumors , indicating that this pathway is closely related to tumor occurrence, metastasis and invasion. (bvsalud.org)
- This review mainly discusses the composition of members in the protein family related to SUMOylation pathways, mutual connections between SUMOylation and other post-translational modifications on proteins as well as therapeutic drugs developed based on these pathways. (bvsalud.org)
- KEPE--a motif frequently superimposed on sumoylation sites in metazoan chromatin proteins and transcription factors. (ox.ac.uk)
- Modest ubiquitin-related modifier 77337-73-6 References proteins (SUMOs) may be covalently conjugated (SUMOylation) to precise lysine residues of several nuclear receptors (a hundred twenty five). (achrinhibitor.com)
- Notably, a latest proteomic screening of SUMOylated proteins from pre- and postischemic brains of mice exposed hyper-SUMOylation of GR right after ischemia (24). (achrinhibitor.com)
- SUMO protein binding to other cellular proteins (SUMOylation) is a key process for many cellular functions. (sciencedaily.com)
- Sumoylation, a post-translational modification involving the covalent conjugation of small ubiquitin-like modifier (SUMO) proteins to a target protein, plays key roles in the modulation of protein functions. (nycu.edu.tw)
- Moreover, YB-1 was found to directly interact with SUMO proteins, and disruption of the SUMO-interacting motif (SIM) of YB-1 not only interfered with this interaction but also diminished YB-1 sumoylation. (nycu.edu.tw)
Regulates5
- 2010). Senp2 also regulates fatty acid metabolism in skeletal Downloaded from https://academic.oup.com/jmcb/article-abstract/10/3/258/4763638 by Ed 'DeepDyve' Gillespie user on 26 June 2018 Senp2 regulates adipose lipid storage by de-SUMOylation of Setdb1 j 259 muscle (Koo et al. (deepdyve.com)
- UBC9 (ubiquitin conjugating enzyme 9), the only known E2 sumoylation enzyme in cells, negatively regulates osteoblastic differentiation induced by BMP (bone morphogenetic protein), partially via sumoylation of SMAD48. (rue2011.com)
- 2020. Caspar SUMOylation regulates lifespan. . (ncbs.res.in)
- Sumoylation regulates exosomal sorting of alpha-Synuclein for extracellular release. (uni-bonn.de)
- SUMOylation regulates cytochrome P450 2E1 expression and activity in alcoholic liver disease. (cedars-sinai.edu)
Protein18
- Though, SUMOylation can affect a substrates' cellular localization, enzymatic activity, or can mediate protein-protein interaction. (ku.edu)
- We further found that SET domain bifurcated 1 (Setdb1) was a SUMOylated protein and that SUMOylation promoted Setdb1 occupancy on the promoter locus of Pparg and Cebpa genes to suppress their expressions by H3K9me3. (deepdyve.com)
- SUMOylation of RPL11 is triggered by ribosomal stress, as well as by alternate reading frame protein upregulation. (sdu.dk)
- Schematic procedure for the EpiQuik In Vivo Universal Protein Sumoylation Assay Kit. (epigentek.com)
- The EpiQuik™ In Vivo Universal Protein Sumoylation Assay Kit is a convenient set of tools that allows the experimenter to measure in vivo protein sumoylation. (epigentek.com)
- The kit is ready-to-use and provides all the essential components needed for measuring in vivo protein sumoylation from multiple mammalian cells/tissues, including human, mouse, and rat. (epigentek.com)
- Included SUMO protein as the positive control allows protein sumoylation to be quantified. (epigentek.com)
- Here we demonstrate that protein SUMOylation is required for insertion of the GluA1 AMPAR subunit following transient glycine-evoked increase in AMPA receptor surface expression (ChemLTP) in dispersed neuronal cultures. (bris.ac.uk)
- Importantly, reducing the extent of substrate protein SUMOylation by overexpressing the deSUMOylating enzyme SENP-1 or inhibiting SUMOylation by expressing dominant negative Ubc9 prevent the ChemLTP-induced increase in both AMPAR surface expression and dendritic SUMO-1 mRNA. (bris.ac.uk)
- Taken together these data demonstrate that SUMOylation of synaptic protein(s) involved in AMPA receptor trafficking is necessary for activity-dependent increases in AMPAR surface expression. (bris.ac.uk)
- Intro Sumoylation is definitely a post-translational changes in which small ubiquitin modifiers (SUMOs) are conjugated to protein targets from the E1, E2, and E3 sumoylation enzymes. (rue2011.com)
- Sumoylation and desumoylation are involved in a variety of cellular processes such as nuclear-to-cytosolic translocation, transcriptional rules, apoptosis, protein stability, response to stress, and stem cell/progenitor maintenance, pluripotency, and differentiation2C6. (rue2011.com)
- Now a team from the Centre for Research in Agricultural Genomics (CRAG), in Spain, has found that the regulation of the protein activity in the plant by the mechanism known as SUMOylation is crucial for the plant protection against fungal infections. (sciencedaily.com)
- Using genetic engineering techniques, the CRAG researchers introduced in the plant a small protein fragment that partially inhibits the SUMOylation. (sciencedaily.com)
- In addition, the researchers observed that shortly after the fungal infection, protein SUMOylation was decreased in the infected plants. (sciencedaily.com)
- This observation suggested that the necrotrophic fungi reduce protein SUMOylation as a mechanism of pathogenicity. (sciencedaily.com)
- The subcellular localization, protein stability, and transcriptional regulatory activity of YB-1 were not significantly affected by sumoylation. (nycu.edu.tw)
- on the protein sumoylation in cardiac regeneration. (portlandpress.com)
Pathway7
- Here, for the first time, we discover that the human SUMOylation pathway is essential for the IBV viral life cycle. (mdpi.com)
- This suggests the possibility that strictly regulated self-renewal mediated by Wnt signaling in cancer cells may be disturbed by the SUMOylation pathway to allow more malignant proliferation. (frontiersin.org)
- To support your research on the role and mechanism of SUMO modifications, Horizon has developed a collection of human knockout HAP1 cell lines that lack components of the SUMOylation pathway. (horizondiscovery.com)
- As a reversible dynamic modification, intracellular sentrin /SUMO-specific proteases (SENPs) mainly regulate the reverse reaction pathway of SUMOylation . (bvsalud.org)
- Results GA obstructed mBMSC osteogenic differentiation To explore the gross aftereffect of the sumoylation pathway in osteogenic differentiation, we decided primary mouse bone tissue marrow stromal cells (mBMSCs) as an experimental model, because they're differentiated into osteoblasts and adipocytes26 readily. (rue2011.com)
- Ginkgolic acidity (GA) was selected to suppress the sumoylation pathway since it was reported being a powerful inhibitor from the sumoylation E1 enzyme21. (rue2011.com)
- Panoramix SUMOylation on chromatin connects the piRNA pathway to the cellular heterochromatin machinery. (oeaw.ac.at)
Chromatin5
- The objectives of this project are to identify nuclear changes in sumoylation during aging and gain mechanistic insight into how altered sumoylation intersects with changes in chromatin, inducibility of stress response, and the consequence on proteostasis and longevity. (rochester.edu)
- Thus, elucidating the intersection between sumoylation, chromatin, and the proteostatic network may have implications for the treatment of neurodegenerative disease and efforts to improve healthy aging. (rochester.edu)
- SUMOylation is a reversible post-translational modification involved in transcription, DNA repair, chromatin remodeling, splicing, assembly of ribosomes and many other cellular processes. (horizondiscovery.com)
- SUMOylation influences Bonus's subnuclear localization, its association with chromatin and interaction with SetDB1. (elifesciences.org)
- Our current genome-wide analyses point out that basal SUMOylation cycles of agonist-bound GR regulate the receptor's chromatin occupancy, enjoying a significant part in managing the antiproliferative result of glucocorticoids (twelve). (achrinhibitor.com)
Inhibition5
- This ERK5-SUMOylation and subsequent inhibition of ERK5 transactivation is one of the mechanisms to explain diabetes-mediated endothelial inflammation and dysfunction (Circ. (mdanderson.org)
- However, until now SUMOylation roles have been difficult to study because, its complete inhibition causes plant death at the seed stage. (sciencedaily.com)
- However, decreased sumoylation disrupted the interaction between YB-1 and PCNA as well as YB-1-mediated inhibition of the MutSα/PCNA interaction and MutSα mismatch binding activity, indicating a functional role of YB-1 sumoylation in inducing DNA mismatch repair (MMR) deficiency and spontaneous mutations. (nycu.edu.tw)
- We further demonstrated that YB-1 sumoylation is crucial for the inhibition of SN1-type alkylator MNNG-induced cytotoxicity, G2/M-phase arrest, apoptosis, and the MMR-dependent DNA damage response. (nycu.edu.tw)
- Lapaquette et al indicate that S flexneri uses a calcium/calpain-dependent mechanism to cause sumoylation inhibition, thereby allowing pathogenic bacterial entry. (medscape.com)
SUMO4
- A post-translational modification with SUMO (SUMOylation) can regulate various cellular events such as DNA replication, repair, transcription and cell cycle regulation. (ku.edu)
- Further, to understand the role of SUMOylation more clearly in human cells we have targeted one of the important SUMOylation enzymes PIASy SUMO E3 ligase. (ku.edu)
- The ratio or intensity of the sumoylation, which is proportional to the conjugated SUMO amount, can be quantified through the signal report-color development system. (epigentek.com)
- Cuerpos esféricos intranucleares sin membrana nucleados por la PROTEÍNA DE LA LEUCEMIA PROMIELOCÍTICA y diversas otras proteínas que contienen un motivo de interacción de modificador pequeño relacionado con la ubiquitina (SUMO, por sus siglas en inglés), o SIM (por sus siglas en inglés), y/o proteínas sumoiladas (por ejemplo, proteína Sp100). (bvsalud.org)
Phosphorylation3
- Not limited to ERK5-SUMOylation, Abe's group also worked on various interesting post-translational modifications including Bcr-mediated PPARg phosphorylation (Circ. (mdanderson.org)
- Leading the Tomasi Lab is Maria Lauda Tomasi, PhD. Tomasi is a pioneer in the fields of sumoylation and phosphorylation in ALD, and more than five years ago she began using a proteomic approach to identify the candidate therapeutic targets. (cedars-sinai.edu)
- SUMOylation and phosphorylation cross-talk in hepatocellular carcinoma. (cedars-sinai.edu)
NEDDylation4
- The Next Frontier: Translational Development of Ubiquitination, SUMOylation, and NEDDylation in Cancer. (ox.ac.uk)
- Novel insights into ubiquitin and ubiquitin-like pathways involved in cancer biology reveal a potential interplay between ubiquitination, SUMOylation, and NEDDylation. (ox.ac.uk)
- This review outlines the current understandings of the regulatory mechanisms and assay capabilities of ubiquitination, SUMOylation, and NEDDylation. (ox.ac.uk)
- It will further highlight the role of ubiquitination, SUMOylation, and NEDDylation in tumorigenesis. (ox.ac.uk)
Ubiquitination2
- With three important enzymes, E1 activating enzyme, E2 conjugating enzyme, and E3 ligase, SUMOylation is mechanistically very similar to ubiquitination. (ku.edu)
- Additional post-translational modifications, such as ubiquitination, sumoylation, acetylation and glycosylation have been detected in STAT5. (nature.com)
Inhibits2
- For example, we) leaves that straight binds to and inhibits the sumoylation E1 enzyme (SAE1/SAE2)21, shows a promising impact in suppressing cancers cell development and migration22C25. (rue2011.com)
- This ERK5-SUMOylation happens at the K6 and K22 sites on the N-terminal region of ERK5, and inhibits ERK5 transcriptional activity. (mdanderson.org)
Glycosylation1
- Predicted post-translational modifications include glycosylation at residues Ser287 and Ser319 and sumoylation at the motifs Phe240 to Gly243, Ala377 to Asp340, and Phe408 to Gly411. (wikipedia.org)
Post-Translational2
- Nucleo-cytosolic partitioning is dependent on the post-translational modifications ubiquitinylation and sumoylation. (biomedcentral.com)
- Recently, Abe's lab team observed a very unique post-translational modification on ERK5, called ERK5-SUMOylation. (mdanderson.org)
Induce2
- We have determined that Topo IIα CTD SUMOylation behaves like a signal transducer to induce a mitotic delay when Topo IIα is catalytically disrupted. (ku.edu)
- Although the exact mechanism remains unclear, high glucose, reactive oxygen species, and advanced glycation end products (AGEs) can induce ERK5-SUMOylation and inhibit ERK5 transactivation. (mdanderson.org)
Inhibitor1
- the effects of garcinol, a HAT inhibitor, differed from those of GA in regulating adipocyte commitment and adipocyte maturation of mBMSCs, implying the GA function in adipogenesis is likely through its activity like a sumoylation inhibitor, not as a HAT inhibitor. (rue2011.com)
Cellular2
- Cellular ubiquitinylation and sumoylation likely influence the functional PTEN loss in high grade lung NET. (biomedcentral.com)
- Therefore, liganded PPARγ sumoylation is not only critical for cellular lipid metabolism but also induces oxidative stress that contributes to tumor suppressive function of PPARγ. (oncotarget.com)
Accumulation1
- Brault ME, Lauzon C, Autexier C. Dyskeratosis congenita mutations in dyskerin SUMOylation consensus sites lead to impaired telomerase RNA accumulation and telomere defects. (medscape.com)
DeSUMOylation1
- SUMOylation and DeSUMOylation: Prospective therapeutic targets in cancer. (bvsalud.org)
Mechanism1
- We have identified inappropriate sumoylation during aging as a potential mechanism to explain loss of stress response inducibility. (rochester.edu)
Induces1
- Additionally, 15d-PGJ2 also 944842-54-0 MedChemExpress induces SUMOylation from the AR (32). (achrinhibitor.com)
Pathways1
- 2013). Dr. Abe made major contributions in analyzing new aspects of signal transduction pathways, especially for SUMOylation, in cardiovascular pathophysiology. (mdanderson.org)
Neurodegenerative diseases2
- Many of the causative factors of neurodegenerative diseases are sumoylated and mutations in core components of the sumoylation machinery are found in AD patients. (rochester.edu)
- For example, in animals, some cancers and neurodegenerative diseases are associated to a defective SUMOylation. (sciencedaily.com)
Modification1
- Hence, some studies have indicated that targeting the SUMOylation modification in Wnt/β-catenin might be a strategy for the treatment cancer ( 24 ). (frontiersin.org)
SENP22
- Senp2 could suppress Setdb1 function by de-SUMOylation. (deepdyve.com)
- Reduced expression of SENP2 increased both p53 and ERK5 SUMOylation, hence increased EC dysfunction and inflammation, and accelerated atherosclerosis formation in vivo. (mdanderson.org)
Inhibit2
- To overcome these limitations, Maria Lois' research group has developed a new tool to inhibit the SUMOylation only partially, so the plant can develop normally. (sciencedaily.com)
- The strategy designed by Maria Lois' team to partially inhibit the SUMOylation has been key in this study, but it is expected that its applications will go much further. (sciencedaily.com)
Studies have indicated1
- Many studies have indicated that SUMOylation is crucial for proper cell cycle progression. (ku.edu)
Regulation2
- Here, we review the complex regulation of Wnt/β-catenin signaling by SUMOylation and discuss the potential targets of SUMOylation therapy. (frontiersin.org)
- More importantly, it turns out that PPARγ regulation of lipid metabolism was dependent on sumoylation of PPARγ. (oncotarget.com)
Extracts1
- Using Xenopus egg extracts (XEEs) we have shown that disruption of mitotic SUMOylation causes chromosome segregation defects. (ku.edu)
Regulator1
- Together, our work identified Bonus as a regulator of tissue-specific gene expression and revealed the importance of SUMOylation as a regulator of complex formation in the context of transcriptional repression. (elifesciences.org)
Lipid1
- Here, we report that sumoylation of PPARγ couples lipid metabolism to tumor suppressive function of the receptor in lung cancer. (oncotarget.com)
Promotes1
- Some evidence suggests that sumoylation promotes adipogenesis. (rue2011.com)
Critical1
- In this study, our results revealed that YB-1 is sumoylated and that Lys26 is a critical residue for YB-1 sumoylation. (nycu.edu.tw)
Cancers1
- Collectively, these results provide molecular explanations for the impact of YB-1 sumoylation on MMR deficiency and alkylator tolerance, which may provide insight for designing therapeutic strategies for malignancies and alkylator-resistant cancers associated with YB-1 overexpression. (nycu.edu.tw)
Consensus1
- MOTIVATION: We noted that the sumoylation site in C/EBP homologues is conserved beyond the canonical consensus sequence for sumoylation. (ox.ac.uk)
Transcriptional1
- Solid evidence, leveraging both in vivo and in vitro studies, reveals the molecular requirements for Bonus' function as a transcriptional repressor, including a key role for sumoylation. (elifesciences.org)
Human2
- Our results suggest that PIASy is an important E3 ligase that mediates mitotic SUMOylation in human cells. (ku.edu)
- Indeed, Maria Lois has already taken steps for transferring the knowledge gained from her plant SUMOylation studies to the field of human health. (sciencedaily.com)
Altogether2
- Altogether, this dissertation research expands our understanding of the significance of SUMOylation during mitosis. (ku.edu)
- Altogether, our results demonstrate a pivotal role for SUMOylation in septin filament bundling and cell division. (pasteur.fr)
Sites2
- Mutation in CTD SUMOylation sites has abrogated the mitotic delay. (ku.edu)
- We then map SUMOylation sites to the C-terminal domain of septins belonging to the SEPT6 and SEPT7 groups and to the N-terminal domain of septins from the SEPT3 group. (pasteur.fr)
Reaction1
- Further, we have shown that disruption of Topo II strand passage reaction (SPR) results in increased Topo IIα SUMOylation and Aurora B mobilization on chromosome arms. (ku.edu)
Molecular1
- We believe that there are still many important SUMOylation functions to discover, and we have designed a molecular tool that will be helpful in this regard," the researcher adds. (sciencedaily.com)
Importantly1
- This new approach will allow us to better understand SUMOylation-regulated processes and, most importantly, it is a tool that can be easily implemented in agronomically important plants, even in those with high genetic complexity, such as wheat," explains Lois. (sciencedaily.com)
Activity3
- An additional study had provided important evidence that blockage of Topo IIα enzymatic activity results in the hyper SUMOylation of Topo IIα. (ku.edu)
- We verified the sumoylation-inhibiting activity of GA in both HEK293 cells and mBMSCs (Fig.?1A). (rue2011.com)
- Specified that 15d-PGJ2 is anti-inflammatory and has an effect on the activity of quite a few nuclear receptors, we sought to ascertain its effects on glucocorticoid signaling as well as the purpose of GR SUMOylation. (achrinhibitor.com)
Function1
- Because sumoylation has a significant function in regulating stem cell differentiation and maintenance, we are motivated to review the function of sumoylation-modulating chemical substances in MSC differentiation. (rue2011.com)
Found3
- Earlier in XEEs, we found that PIASy is an essentially important E3 ligase for mitotic SUMOylation. (ku.edu)
- Very recently Abe's group found that disturbed flow induced SUMOylation of p53 and ERK5, leading to ECs apoptosis and inflammation, respectively. (mdanderson.org)
- Using this new approach, CRAG's team found that plants with compromised SUMOylation showed an increased susceptibility to necrotrophic fungal infections by Botrytis cinerea and Plectosphaerella cucumerina . (sciencedaily.com)
Explore1
- This project will explore how changes in sumoylation during aging alter the epigenome, inducibility of stress responses, and maintenance of proteostasis. (rochester.edu)